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elNémo ID: 22031315571861151

Job options:

ID        	=	 22031315571861151
JOBID     	=	 
USERID    	=	 unknown
PRIVAT    	=	 0

NMODES    	=	 5
DQMIN     	=	 -100
DQMAX     	=	 100
DQSTEP    	=	 20
DOGRAPHS  	=	 on

DOPROJMODS	=	 0
DORMSD    	=	 0

NRBL      	=	 0
CUTOFF    	=	 0
CAONLY    	=	 0


Input data for this run:


REMARK    File generated by Swiss-PdbViewer  4.00b0
REMARK    http://www.expasy.org/spdbv/
REMARK    File generated by Swiss-PdbViewer  4.00b0
REMARK    http://www.expasy.org/spdbv/
REMARK    File generated by Swiss-PdbViewer  4.00b0
REMARK    http://www.expasy.org/spdbv/
TITLE     SWISS-MODEL SERVER (https://swissmodel.expasy.org)
TITLE    2 PREDICTEDinsulin-likegrowthfactor1receptorOreochromisniloticusNCBIRef
TITLE    3 erenceSequenceXP_003440646.2
EXPDTA    THEORETICAL MODEL (SWISS-MODEL SERVER)
AUTHOR    SWISS-MODEL SERVER (SEE REFERENCE IN JRNL Records)
REVDAT   1   05-JUL-18 1MOD    1       10:46
REMARK   1
REMARK   1 REFERENCE 1
REMARK   1  AUTH   S.BIENERT,A.WATERHOUSE,T.A.P.DE BEER,G.TAURIELLO,G.STUDER,
REMARK   1  AUTH 2 L.BORDOLI,T.SCHWEDE
REMARK   1  TITL   THE SWISS-MODEL REPOSITORY - NEW FEATURES AND FUNCTIONALITY
REMARK   1  REF    NUCLEIC.ACIDS.RES..           V.  22       2017
REMARK   1  REFN                   ISSN 0305-1048
REMARK   1  PMID   27899672
REMARK   1  DOI    10.1093/nar/gkw1132
REMARK   1
REMARK   1 REFERENCE 2
REMARK   1  AUTH   N.GUEX,M.C.PEITSCH,T.SCHWEDE
REMARK   1  TITL   AUTOMATED COMPARATIVE PROTEIN STRUCTURE MODELING WITH
REMARK   1  TITL 2 SWISS-MODEL AND SWISS-PDBVIEWER: A HISTORICAL PERSPECTIVE
REMARK   1  REF    ELECTROPHORESIS               V.30         2009
REMARK   1  REFN                   ISSN 0173-0835
REMARK   1  PMID   19517507
REMARK   1  DOI    10.1002/elps.200900140
REMARK   1
REMARK   1 REFERENCE 3
REMARK   1  AUTH   P.BENKERT,M.BIASINI,T.SCHWEDE
REMARK   1  TITL   TOWARD THE ESTIMATION OF THE ABSOLUTE QUALITY OF INDIVIDUAL
REMARK   1  TITL 2 PROTEIN STRUCTURE MODELS
REMARK   1  REF    BIOINFORMATICS                V.27         2011
REMARK   1  REFN                   ISSN 1367-4803
REMARK   1  PMID   21134891
REMARK   1  DOI    10.1093/bioinformatics/btq662
REMARK   1
REMARK   1 REFERENCE 4
REMARK   1  AUTH   M.BERTONI,F.KIEFER,M.BIASINI,L.BORDOLI,T.SCHWEDE
REMARK   1  TITL   MODELING PROTEIN QUATERNARY STRUCTURE OF HOMO- AND
REMARK   1  TITL 2 HETERO-OLIGOMERS BEYOND BINARY INTERACTIONS BY HOMOLOGY
REMARK   1  REF    SCI.REP.                      V. 7         2017
REMARK   1  REFN                   ISSN
REMARK   1  PMID   28874689
REMARK   1  DOI    10.1038/s41598-017-09654-8
REMARK   1
REMARK   1 DISCLAIMER
REMARK   1 The SWISS-MODEL SERVER produces theoretical models for proteins.
REMARK   1 The results of any theoretical modelling procedure is
REMARK   1 NON-EXPERIMENTAL and MUST be considered with care. These models may
REMARK   1 contain significant errors. This is especially true for automated
REMARK   1 modeling since there is no human intervention during model
REMARK   1 building. Please read the header section and the logfile carefully
REMARK   1 to know what templates and alignments were used during the model
REMARK   1 building process. All information by the SWISS-MODEL SERVER is
REMARK   1 provided "AS-IS", without any warranty, expressed or implied.
REMARK   2
REMARK   2 COPYRIGHT NOTICE
REMARK   2 This SWISS-MODEL protein model is copyright. It is produced by the
REMARK   2 SWISS-MODEL server, developed by the Computational Structural
REMARK   2 Biology Group at the SIB Swiss Institute of Bioinformatics at the
REMARK   2 Biozentrum, University of Basel (https://swissmodel.expasy.org). This
REMARK   2 model is licensed under the CC BY-SA 4.0 Creative Commons
REMARK   2 Attribution-ShareAlike 4.0 International License
REMARK   2 (https://creativecommons.org/licenses/by-sa/4.0/legalcode), i.e. you
REMARK   2 can copy and redistribute the model in any medium or format,
REMARK   2 transform and build upon the model for any purpose, even
REMARK   2 commercially, under the following terms:
REMARK   2 Attribution - You must give appropriate credit, provide a link to
REMARK   2 the license, and indicate if changes were made. You may do so in any
REMARK   2 reasonable manner, but not in any way that suggests the licensor
REMARK   2 endorses you or your use. When you publish, patent or distribute
REMARK   2 results that were fully or partially based on the model, please cite
REMARK   2 the corresponding papers mentioned under JRNL.
REMARK   2 ShareAlike - If you remix, transform, or build upon the material,
REMARK   2 you must distribute your contributions under the same license as the
REMARK   2 original.
REMARK   2 No additional restrictions - you may not apply legal terms or
REMARK   2 technological measures that legally restrict others from doing
REMARK   2 anything the license permits.
REMARK   2 Find a human-readable summary of (and not a substitute for) the
REMARK   2 CC BY-SA 4.0 license at this link:
REMARK   2 https://creativecommons.org/licenses/by-sa/4.0/
REMARK   3 
REMARK   3 MODEL INFORMATION
REMARK   3  ENGIN   PROMOD3
REMARK   3  VERSN   1.1.0
REMARK   3  OSTAT   monomer
REMARK   3  OSRSN   PREDICTION
REMARK   3  QSPRD   0.413
REMARK   3  GMQE    0.49
REMARK   3  QMN4    -3.21
REMARK   3  MODT    FALSE
REMARK   3 
REMARK   3 TEMPLATE 1
REMARK   3  PDBID   5u8q
REMARK   3  CHAIN   A
REMARK   3  MMCIF   A
REMARK   3  PDBV    2018-06-22
REMARK   3  SMTLE   5u8q.1.A
REMARK   3  SMTLV   2018-06-29
REMARK   3  MTHD    X-RAY DIFFRACTION 3.27 A
REMARK   3  FOUND   BLAST
REMARK   3  GMQE    0.49
REMARK   3  SIM     0.50
REMARK   3  SID     62.63
REMARK   3  OSTAT   homo-dimer
REMARK   3  LIGND   MLT
REMARK   3  LIGND 2 MLT
REMARK   3  LIGND 3 NAG
REMARK   3  LIGND 4 NAG
REMARK   3  LIGND 5 NAG
REMARK   3  LIGND 6 NAG
REMARK   3  LIGND 7 NAG
REMARK   3  LIGND 8 NAG
REMARK   3  LIGND 9 NAG
REMARK   3  LIGND 10 NAG
REMARK   3  LIGND 11 NAG
REMARK   3  LIGND 12 NAG
REMARK   3  LIGND 13 NAG
REMARK   3  LIGND 14 NAG
REMARK   3  LIGND 15 NAG
REMARK   3  LIGND 16 NAG
REMARK   3  LIGND 17 NAG
REMARK   3  LIGND 18 NAG
ATOM      1  N   GLU A  35      29.998  43.702 -41.319  1.00  0.75
ATOM      2  CA  GLU A  35      28.689  43.366 -40.697  1.00  0.75
ATOM      3  C   GLU A  35      28.415  41.889 -40.573  1.00  0.75
ATOM      4  O   GLU A  35      28.454  41.168 -41.568  1.00  0.75
ATOM      5  CB  GLU A  35      27.582  44.082 -41.511  1.00  0.75
ATOM      6  CG  GLU A  35      26.168  43.948 -40.902  1.00  0.75
ATOM      7  CD  GLU A  35      26.053  44.507 -39.487  1.00  0.75
ATOM      8  OE1 GLU A  35      27.080  44.994 -38.948  1.00  0.75
ATOM      9  OE2 GLU A  35      24.930  44.421 -38.941  1.00  0.75
ATOM     10  N   ILE A  36      28.177  41.398 -39.343  1.00  0.87
ATOM     11  CA  ILE A  36      27.996  39.983 -39.065  1.00  0.87
ATOM     12  C   ILE A  36      26.619  39.873 -38.472  1.00  0.87
ATOM     13  O   ILE A  36      26.346  40.431 -37.414  1.00  0.87
ATOM     14  CB  ILE A  36      28.999  39.378 -38.070  1.00  0.87
ATOM     15  CG1 ILE A  36      30.469  39.583 -38.508  1.00  0.87
ATOM     16  CG2 ILE A  36      28.693  37.872 -37.878  1.00  0.87
ATOM     17  CD1 ILE A  36      31.477  39.141 -37.434  1.00  0.87
ATOM     18  N   CYS A  37      25.714  39.159 -39.152  1.00  0.87
ATOM     19  CA  CYS A  37      24.326  39.083 -38.747  1.00  0.87
ATOM     20  C   CYS A  37      24.054  37.689 -38.234  1.00  0.87
ATOM     21  O   CYS A  37      24.393  36.718 -38.900  1.00  0.87
ATOM     22  CB  CYS A  37      23.392  39.363 -39.950  1.00  0.87
ATOM     23  SG  CYS A  37      23.543  41.065 -40.571  1.00  0.87
ATOM     24  N   GLY A  38      23.458  37.537 -37.033  1.00  0.86
ATOM     25  CA  GLY A  38      23.259  36.210 -36.465  1.00  0.86
ATOM     26  C   GLY A  38      22.585  36.240 -35.122  1.00  0.86
ATOM     27  O   GLY A  38      21.976  37.253 -34.778  1.00  0.86
ATOM     28  N   PRO A  39      22.656  35.173 -34.323  1.00  0.79
ATOM     29  CA  PRO A  39      23.245  33.872 -34.630  1.00  0.79
ATOM     30  C   PRO A  39      22.404  33.010 -35.531  1.00  0.79
ATOM     31  O   PRO A  39      22.897  31.962 -35.903  1.00  0.79
ATOM     32  CB  PRO A  39      23.408  33.181 -33.262  1.00  0.79
ATOM     33  CG  PRO A  39      22.859  34.170 -32.225  1.00  0.79
ATOM     34  CD  PRO A  39      21.989  35.132 -33.032  1.00  0.79
ATOM     35  N   ASP A  40      21.163  33.397 -35.864  1.00  0.81
ATOM     36  CA  ASP A  40      20.330  32.639 -36.766  1.00  0.81
ATOM     37  C   ASP A  40      19.456  33.637 -37.501  1.00  0.81
ATOM     38  O   ASP A  40      19.059  34.649 -36.919  1.00  0.81
ATOM     39  CB  ASP A  40      19.409  31.668 -35.988  1.00  0.81
ATOM     40  CG  ASP A  40      20.223  30.514 -35.437  1.00  0.81
ATOM     41  OD1 ASP A  40      21.006  29.925 -36.227  1.00  0.81
ATOM     42  OD2 ASP A  40      20.007  30.161 -34.249  1.00  0.81
ATOM     43  N   ILE A  41      19.122  33.421 -38.793  1.00  0.85
ATOM     44  CA  ILE A  41      18.169  34.274 -39.497  1.00  0.85
ATOM     45  C   ILE A  41      17.006  33.441 -40.041  1.00  0.85
ATOM     46  O   ILE A  41      17.155  32.693 -41.004  1.00  0.85
ATOM     47  CB  ILE A  41      18.797  35.094 -40.635  1.00  0.85
ATOM     48  CG1 ILE A  41      20.059  35.897 -40.214  1.00  0.85
ATOM     49  CG2 ILE A  41      17.743  36.047 -41.241  1.00  0.85
ATOM     50  CD1 ILE A  41      19.850  36.985 -39.149  1.00  0.85
ATOM     51  N   ASP A  42      15.782  33.590 -39.476  1.00  0.85
ATOM     52  CA  ASP A  42      14.557  33.071 -40.073  1.00  0.85
ATOM     53  C   ASP A  42      13.736  34.246 -40.609  1.00  0.85
ATOM     54  O   ASP A  42      13.518  35.240 -39.907  1.00  0.85
ATOM     55  CB  ASP A  42      13.777  32.117 -39.097  1.00  0.85
ATOM     56  CG  ASP A  42      12.637  31.342 -39.741  1.00  0.85
ATOM     57  OD1 ASP A  42      11.687  31.971 -40.265  1.00  0.85
ATOM     58  OD2 ASP A  42      12.646  30.083 -39.687  1.00  0.85
ATOM     59  N   LEU A  43      13.341  34.170 -41.900  1.00  0.80
ATOM     60  CA  LEU A  43      12.595  35.146 -42.665  1.00  0.80
ATOM     61  C   LEU A  43      11.436  34.435 -43.323  1.00  0.80
ATOM     62  O   LEU A  43      11.610  33.526 -44.139  1.00  0.80
ATOM     63  CB  LEU A  43      13.433  35.849 -43.783  1.00  0.80
ATOM     64  CG  LEU A  43      14.712  36.534 -43.259  1.00  0.80
ATOM     65  CD1 LEU A  43      15.616  37.119 -44.353  1.00  0.80
ATOM     66  CD2 LEU A  43      14.424  37.563 -42.172  1.00  0.80
ATOM     67  N   ARG A  44      10.201  34.833 -42.983  1.00  0.73
ATOM     68  CA  ARG A  44       9.047  34.093 -43.422  1.00  0.73
ATOM     69  C   ARG A  44       7.813  34.955 -43.421  1.00  0.73
ATOM     70  O   ARG A  44       7.783  36.012 -42.790  1.00  0.73
ATOM     71  CB  ARG A  44       8.792  32.844 -42.538  1.00  0.73
ATOM     72  CG  ARG A  44       8.516  33.161 -41.056  1.00  0.73
ATOM     73  CD  ARG A  44       8.030  31.949 -40.260  1.00  0.73
ATOM     74  NE  ARG A  44       9.198  31.050 -40.051  1.00  0.73
ATOM     75  CZ  ARG A  44       9.152  29.788 -39.621  1.00  0.73
ATOM     76  NH1 ARG A  44       8.003  29.193 -39.334  1.00  0.73
ATOM     77  NH2 ARG A  44      10.283  29.114 -39.450  1.00  0.73
ATOM     78  N   GLY A  45       6.762  34.496 -44.133  1.00  0.64
ATOM     79  CA  GLY A  45       5.463  35.139 -44.237  1.00  0.64
ATOM     80  C   GLY A  45       5.527  36.374 -45.133  1.00  0.64
ATOM     81  O   GLY A  45       5.275  36.319 -46.334  1.00  0.64
ATOM     82  N   ASP A  46       5.886  37.532 -44.558  1.00  0.63
ATOM     83  CA  ASP A  46       6.008  38.784 -45.256  1.00  0.63
ATOM     84  C   ASP A  46       7.159  38.832 -46.250  1.00  0.63
ATOM     85  O   ASP A  46       8.322  38.600 -45.920  1.00  0.63
ATOM     86  CB  ASP A  46       6.230  39.927 -44.248  1.00  0.63
ATOM     87  CG  ASP A  46       5.098  39.952 -43.249  1.00  0.63
ATOM     88  OD1 ASP A  46       3.974  40.334 -43.656  1.00  0.63
ATOM     89  OD2 ASP A  46       5.356  39.562 -42.077  1.00  0.63
ATOM     90  N   ILE A  47       6.865  39.230 -47.499  1.00  0.63
ATOM     91  CA  ILE A  47       7.853  39.469 -48.535  1.00  0.63
ATOM     92  C   ILE A  47       8.862  40.564 -48.171  1.00  0.63
ATOM     93  O   ILE A  47      10.063  40.460 -48.420  1.00  0.63
ATOM     94  CB  ILE A  47       7.163  39.763 -49.867  1.00  0.63
ATOM     95  CG1 ILE A  47       6.338  41.074 -49.897  1.00  0.63
ATOM     96  CG2 ILE A  47       6.287  38.559 -50.275  1.00  0.63
ATOM     97  CD1 ILE A  47       5.866  41.457 -51.304  1.00  0.63
ATOM     98  N   ASP A  48       8.387  41.627 -47.493  1.00  0.71
ATOM     99  CA  ASP A  48       9.154  42.797 -47.136  1.00  0.71
ATOM    100  C   ASP A  48      10.008  42.556 -45.883  1.00  0.71
ATOM    101  O   ASP A  48      10.890  43.344 -45.539  1.00  0.71
ATOM    102  CB  ASP A  48       8.175  43.991 -46.951  1.00  0.71
ATOM    103  CG  ASP A  48       7.518  44.409 -48.269  1.00  0.71
ATOM    104  OD1 ASP A  48       8.135  44.221 -49.349  1.00  0.71
ATOM    105  OD2 ASP A  48       6.376  44.938 -48.219  1.00  0.71
ATOM    106  N   GLN A  49       9.841  41.398 -45.197  1.00  0.70
ATOM    107  CA  GLN A  49      10.673  41.003 -44.068  1.00  0.70
ATOM    108  C   GLN A  49      12.081  40.588 -44.494  1.00  0.70
ATOM    109  O   GLN A  49      13.002  40.514 -43.680  1.00  0.70
ATOM    110  CB  GLN A  49       9.982  39.900 -43.222  1.00  0.70
ATOM    111  CG  GLN A  49      10.593  39.685 -41.816  1.00  0.70
ATOM    112  CD  GLN A  49       9.902  38.609 -40.974  1.00  0.70
ATOM    113  OE1 GLN A  49      10.617  37.789 -40.388  1.00  0.70
ATOM    114  NE2 GLN A  49       8.556  38.632 -40.860  1.00  0.70
ATOM    115  N   PHE A  50      12.320  40.395 -45.811  1.00  0.77
ATOM    116  CA  PHE A  50      13.652  40.193 -46.360  1.00  0.77
ATOM    117  C   PHE A  50      14.593  41.334 -46.198  1.00  0.77
ATOM    118  O   PHE A  50      15.805  41.145 -46.243  1.00  0.77
ATOM    119  CB  PHE A  50      13.606  39.909 -47.876  1.00  0.77
ATOM    120  CG  PHE A  50      13.217  38.488 -48.137  1.00  0.77
ATOM    121  CD1 PHE A  50      13.491  37.416 -47.272  1.00  0.77
ATOM    122  CD2 PHE A  50      12.483  38.234 -49.292  1.00  0.77
ATOM    123  CE1 PHE A  50      12.971  36.143 -47.513  1.00  0.77
ATOM    124  CE2 PHE A  50      12.017  36.959 -49.583  1.00  0.77
ATOM    125  CZ  PHE A  50      12.238  35.924 -48.689  1.00  0.77
ATOM    126  N   LYS A  51      14.076  42.538 -45.950  1.00  0.81
ATOM    127  CA  LYS A  51      14.881  43.711 -45.771  1.00  0.81
ATOM    128  C   LYS A  51      15.974  43.596 -44.701  1.00  0.81
ATOM    129  O   LYS A  51      17.025  44.208 -44.820  1.00  0.81
ATOM    130  CB  LYS A  51      13.943  44.892 -45.522  1.00  0.81
ATOM    131  CG  LYS A  51      14.625  46.205 -45.868  1.00  0.81
ATOM    132  CD  LYS A  51      13.738  47.392 -45.532  1.00  0.81
ATOM    133  CE  LYS A  51      14.504  48.681 -45.785  1.00  0.81
ATOM    134  NZ  LYS A  51      13.672  49.812 -45.356  1.00  0.81
ATOM    135  N   ARG A  52      15.805  42.708 -43.691  1.00  0.80
ATOM    136  CA  ARG A  52      16.793  42.395 -42.662  1.00  0.80
ATOM    137  C   ARG A  52      18.185  41.959 -43.153  1.00  0.80
ATOM    138  O   ARG A  52      19.120  41.890 -42.361  1.00  0.80
ATOM    139  CB  ARG A  52      16.256  41.259 -41.731  1.00  0.80
ATOM    140  CG  ARG A  52      15.028  41.663 -40.878  1.00  0.80
ATOM    141  CD  ARG A  52      14.176  40.520 -40.285  1.00  0.80
ATOM    142  NE  ARG A  52      15.041  39.631 -39.443  1.00  0.80
ATOM    143  CZ  ARG A  52      14.650  38.461 -38.915  1.00  0.80
ATOM    144  NH1 ARG A  52      13.411  37.988 -39.009  1.00  0.80
ATOM    145  NH2 ARG A  52      15.545  37.708 -38.277  1.00  0.80
ATOM    146  N   LEU A  53      18.373  41.675 -44.459  1.00  0.84
ATOM    147  CA  LEU A  53      19.659  41.329 -45.032  1.00  0.84
ATOM    148  C   LEU A  53      20.333  42.515 -45.722  1.00  0.84
ATOM    149  O   LEU A  53      21.388  42.355 -46.331  1.00  0.84
ATOM    150  CB  LEU A  53      19.500  40.144 -46.022  1.00  0.84
ATOM    151  CG  LEU A  53      18.845  38.888 -45.399  1.00  0.84
ATOM    152  CD1 LEU A  53      18.603  37.801 -46.458  1.00  0.84
ATOM    153  CD2 LEU A  53      19.655  38.315 -44.223  1.00  0.84
ATOM    154  N   GLU A  54      19.783  43.749 -45.605  1.00  0.83
ATOM    155  CA  GLU A  54      20.278  44.966 -46.247  1.00  0.83
ATOM    156  C   GLU A  54      21.734  45.317 -45.956  1.00  0.83
ATOM    157  O   GLU A  54      22.475  45.728 -46.851  1.00  0.83
ATOM    158  CB  GLU A  54      19.341  46.184 -45.983  1.00  0.83
ATOM    159  CG  GLU A  54      19.087  46.604 -44.506  1.00  0.83
ATOM    160  CD  GLU A  54      17.952  47.633 -44.414  1.00  0.83
ATOM    161  OE1 GLU A  54      18.026  48.687 -45.099  1.00  0.83
ATOM    162  OE2 GLU A  54      16.965  47.374 -43.675  1.00  0.83
ATOM    163  N   ASN A  55      22.208  45.118 -44.711  1.00  0.85
ATOM    164  CA  ASN A  55      23.593  45.398 -44.367  1.00  0.85
ATOM    165  C   ASN A  55      24.485  44.158 -44.298  1.00  0.85
ATOM    166  O   ASN A  55      25.712  44.266 -44.316  1.00  0.85
ATOM    167  CB  ASN A  55      23.644  46.080 -42.980  1.00  0.85
ATOM    168  CG  ASN A  55      22.802  47.347 -43.006  1.00  0.85
ATOM    169  OD1 ASN A  55      22.878  48.142 -43.945  1.00  0.85
ATOM    170  ND2 ASN A  55      21.970  47.543 -41.960  1.00  0.85
ATOM    171  N   CYS A  56      23.906  42.946 -44.219  1.00  0.87
ATOM    172  CA  CYS A  56      24.630  41.727 -43.877  1.00  0.87
ATOM    173  C   CYS A  56      25.608  41.234 -44.939  1.00  0.87
ATOM    174  O   CYS A  56      25.219  40.900 -46.053  1.00  0.87
ATOM    175  CB  CYS A  56      23.656  40.567 -43.552  1.00  0.87
ATOM    176  SG  CYS A  56      22.447  41.029 -42.275  1.00  0.87
ATOM    177  N   THR A  57      26.914  41.137 -44.606  1.00  0.87
ATOM    178  CA  THR A  57      27.919  40.564 -45.514  1.00  0.87
ATOM    179  C   THR A  57      28.219  39.124 -45.148  1.00  0.87
ATOM    180  O   THR A  57      28.464  38.275 -46.006  1.00  0.87
ATOM    181  CB  THR A  57      29.194  41.420 -45.618  1.00  0.87
ATOM    182  OG1 THR A  57      30.271  40.779 -46.288  1.00  0.87
ATOM    183  CG2 THR A  57      29.734  41.831 -44.244  1.00  0.87
ATOM    184  N   VAL A  58      28.112  38.787 -43.852  1.00  0.89
ATOM    185  CA  VAL A  58      28.302  37.434 -43.374  1.00  0.89
ATOM    186  C   VAL A  58      27.111  37.080 -42.523  1.00  0.89
ATOM    187  O   VAL A  58      26.751  37.811 -41.596  1.00  0.89
ATOM    188  CB  VAL A  58      29.584  37.273 -42.566  1.00  0.89
ATOM    189  CG1 VAL A  58      29.761  35.808 -42.109  1.00  0.89
ATOM    190  CG2 VAL A  58      30.775  37.704 -43.445  1.00  0.89
ATOM    191  N   VAL A  59      26.456  35.944 -42.823  1.00  0.89
ATOM    192  CA  VAL A  59      25.378  35.439 -41.994  1.00  0.89
ATOM    193  C   VAL A  59      25.962  34.383 -41.103  1.00  0.89
ATOM    194  O   VAL A  59      26.369  33.306 -41.544  1.00  0.89
ATOM    195  CB  VAL A  59      24.194  34.875 -42.762  1.00  0.89
ATOM    196  CG1 VAL A  59      23.120  34.335 -41.793  1.00  0.89
ATOM    197  CG2 VAL A  59      23.591  36.008 -43.610  1.00  0.89
ATOM    198  N   GLU A  60      26.024  34.694 -39.802  1.00  0.85
ATOM    199  CA  GLU A  60      26.474  33.774 -38.799  1.00  0.85
ATOM    200  C   GLU A  60      25.285  32.926 -38.428  1.00  0.85
ATOM    201  O   GLU A  60      24.255  33.455 -38.021  1.00  0.85
ATOM    202  CB  GLU A  60      27.091  34.530 -37.600  1.00  0.85
ATOM    203  CG  GLU A  60      28.075  33.683 -36.761  1.00  0.85
ATOM    204  CD  GLU A  60      29.025  34.540 -35.936  1.00  0.85
ATOM    205  OE1 GLU A  60      28.554  35.382 -35.133  1.00  0.85
ATOM    206  OE2 GLU A  60      30.272  34.412 -36.097  1.00  0.85
ATOM    207  N   GLY A  61      25.374  31.604 -38.647  1.00  0.88
ATOM    208  CA  GLY A  61      24.288  30.672 -38.424  1.00  0.88
ATOM    209  C   GLY A  61      23.641  30.150 -39.655  1.00  0.88
ATOM    210  O   GLY A  61      24.255  30.022 -40.713  1.00  0.88
ATOM    211  N   TYR A  62      22.350  29.796 -39.544  1.00  0.86
ATOM    212  CA  TYR A  62      21.555  29.390 -40.685  1.00  0.86
ATOM    213  C   TYR A  62      20.774  30.547 -41.278  1.00  0.86
ATOM    214  O   TYR A  62      20.515  31.568 -40.640  1.00  0.86
ATOM    215  CB  TYR A  62      20.639  28.160 -40.405  1.00  0.86
ATOM    216  CG  TYR A  62      19.594  28.383 -39.348  1.00  0.86
ATOM    217  CD1 TYR A  62      18.451  29.142 -39.623  1.00  0.86
ATOM    218  CD2 TYR A  62      19.736  27.842 -38.067  1.00  0.86
ATOM    219  CE1 TYR A  62      17.499  29.394 -38.626  1.00  0.86
ATOM    220  CE2 TYR A  62      18.826  28.142 -37.046  1.00  0.86
ATOM    221  CZ  TYR A  62      17.705  28.923 -37.328  1.00  0.86
ATOM    222  OH  TYR A  62      16.808  29.290 -36.306  1.00  0.86
ATOM    223  N   LEU A  63      20.344  30.378 -42.539  1.00  0.89
ATOM    224  CA  LEU A  63      19.413  31.282 -43.179  1.00  0.89
ATOM    225  C   LEU A  63      18.188  30.505 -43.635  1.00  0.89
ATOM    226  O   LEU A  63      18.274  29.532 -44.388  1.00  0.89
ATOM    227  CB  LEU A  63      20.092  32.031 -44.353  1.00  0.89
ATOM    228  CG  LEU A  63      19.216  33.030 -45.150  1.00  0.89
ATOM    229  CD1 LEU A  63      18.513  34.078 -44.272  1.00  0.89
ATOM    230  CD2 LEU A  63      20.081  33.758 -46.192  1.00  0.89
ATOM    231  N   ARG A  64      16.997  30.917 -43.159  1.00  0.87
ATOM    232  CA  ARG A  64      15.721  30.374 -43.583  1.00  0.87
ATOM    233  C   ARG A  64      14.937  31.409 -44.352  1.00  0.87
ATOM    234  O   ARG A  64      14.714  32.520 -43.880  1.00  0.87
ATOM    235  CB  ARG A  64      14.795  29.961 -42.415  1.00  0.87
ATOM    236  CG  ARG A  64      15.359  28.918 -41.456  1.00  0.87
ATOM    237  CD  ARG A  64      15.659  27.593 -42.130  1.00  0.87
ATOM    238  NE  ARG A  64      15.920  26.606 -41.045  1.00  0.87
ATOM    239  CZ  ARG A  64      14.957  25.945 -40.392  1.00  0.87
ATOM    240  NH1 ARG A  64      15.318  25.031 -39.501  1.00  0.87
ATOM    241  NH2 ARG A  64      13.667  26.184 -40.596  1.00  0.87
ATOM    242  N   ILE A  65      14.482  31.037 -45.558  1.00  0.85
ATOM    243  CA  ILE A  65      13.646  31.851 -46.410  1.00  0.85
ATOM    244  C   ILE A  65      12.430  30.999 -46.771  1.00  0.85
ATOM    245  O   ILE A  65      12.490  30.118 -47.632  1.00  0.85
ATOM    246  CB  ILE A  65      14.497  32.254 -47.610  1.00  0.85
ATOM    247  CG1 ILE A  65      15.627  33.196 -47.135  1.00  0.85
ATOM    248  CG2 ILE A  65      13.657  32.895 -48.719  1.00  0.85
ATOM    249  CD1 ILE A  65      16.387  33.870 -48.272  1.00  0.85
ATOM    250  N   LEU A  66      11.295  31.199 -46.059  1.00  0.81
ATOM    251  CA  LEU A  66      10.209  30.215 -45.997  1.00  0.81
ATOM    252  C   LEU A  66       8.827  30.846 -46.188  1.00  0.81
ATOM    253  O   LEU A  66       8.486  31.830 -45.540  1.00  0.81
ATOM    254  CB  LEU A  66      10.143  29.511 -44.600  1.00  0.81
ATOM    255  CG  LEU A  66      11.078  28.317 -44.281  1.00  0.81
ATOM    256  CD1 LEU A  66      12.478  28.377 -44.879  1.00  0.81
ATOM    257  CD2 LEU A  66      11.222  28.221 -42.756  1.00  0.81
ATOM    258  N   LEU A  67       7.966  30.272 -47.063  1.00  0.71
ATOM    259  CA  LEU A  67       6.528  30.569 -47.120  1.00  0.71
ATOM    260  C   LEU A  67       6.200  31.985 -47.544  1.00  0.71
ATOM    261  O   LEU A  67       5.336  32.672 -47.005  1.00  0.71
ATOM    262  CB  LEU A  67       5.787  30.234 -45.805  1.00  0.71
ATOM    263  CG  LEU A  67       5.945  28.777 -45.343  1.00  0.71
ATOM    264  CD1 LEU A  67       5.342  28.638 -43.944  1.00  0.71
ATOM    265  CD2 LEU A  67       5.285  27.794 -46.320  1.00  0.71
ATOM    266  N   ILE A  68       6.917  32.425 -48.574  1.00  0.68
ATOM    267  CA  ILE A  68       6.990  33.792 -49.021  1.00  0.68
ATOM    268  C   ILE A  68       6.137  33.846 -50.267  1.00  0.68
ATOM    269  O   ILE A  68       6.624  33.865 -51.393  1.00  0.68
ATOM    270  CB  ILE A  68       8.443  34.180 -49.326  1.00  0.68
ATOM    271  CG1 ILE A  68       9.392  33.830 -48.141  1.00  0.68
ATOM    272  CG2 ILE A  68       8.475  35.667 -49.752  1.00  0.68
ATOM    273  CD1 ILE A  68       9.281  34.826 -46.999  1.00  0.68
ATOM    274  N   ASN A  69       4.813  33.790 -50.102  1.00  0.56
ATOM    275  CA  ASN A  69       3.890  33.750 -51.207  1.00  0.56
ATOM    276  C   ASN A  69       2.941  34.890 -50.923  1.00  0.56
ATOM    277  O   ASN A  69       3.350  36.043 -50.818  1.00  0.56
ATOM    278  CB  ASN A  69       3.238  32.329 -51.282  1.00  0.56
ATOM    279  CG  ASN A  69       2.356  32.144 -52.511  1.00  0.56
ATOM    280  OD1 ASN A  69       2.278  32.996 -53.393  1.00  0.56
ATOM    281  ND2 ASN A  69       1.666  30.987 -52.595  1.00  0.56
ATOM    282  N   GLU A  70       1.657  34.583 -50.741  1.00  0.38
ATOM    283  CA  GLU A  70       0.658  35.443 -50.181  1.00  0.38
ATOM    284  C   GLU A  70       1.003  35.985 -48.797  1.00  0.38
ATOM    285  O   GLU A  70       1.651  35.321 -47.990  1.00  0.38
ATOM    286  CB  GLU A  70      -0.620  34.595 -50.038  1.00  0.38
ATOM    287  CG  GLU A  70      -1.106  33.940 -51.356  1.00  0.38
ATOM    288  CD  GLU A  70      -1.631  34.901 -52.421  1.00  0.38
ATOM    289  OE1 GLU A  70      -1.718  36.132 -52.179  1.00  0.38
ATOM    290  OE2 GLU A  70      -1.966  34.366 -53.507  1.00  0.38
ATOM    291  N   LYS A  71       0.529  37.197 -48.447  1.00  0.39
ATOM    292  CA  LYS A  71       0.757  37.822 -47.151  1.00  0.39
ATOM    293  C   LYS A  71      -0.182  37.278 -46.071  1.00  0.39
ATOM    294  O   LYS A  71      -0.737  38.035 -45.289  1.00  0.39
ATOM    295  CB  LYS A  71       0.601  39.372 -47.235  1.00  0.39
ATOM    296  CG  LYS A  71       1.328  40.075 -48.404  1.00  0.39
ATOM    297  CD  LYS A  71       0.874  41.547 -48.529  1.00  0.39
ATOM    298  CE  LYS A  71       1.642  42.404 -49.544  1.00  0.39
ATOM    299  NZ  LYS A  71       1.104  43.785 -49.508  1.00  0.39
ATOM    300  N   THR A  72      -0.370  35.948 -46.014  1.00  0.35
ATOM    301  CA  THR A  72      -1.203  35.129 -45.129  1.00  0.35
ATOM    302  C   THR A  72      -1.694  33.993 -46.030  1.00  0.35
ATOM    303  O   THR A  72      -0.962  33.047 -46.292  1.00  0.35
ATOM    304  CB  THR A  72      -2.368  35.779 -44.335  1.00  0.35
ATOM    305  OG1 THR A  72      -1.915  36.781 -43.428  1.00  0.35
ATOM    306  CG2 THR A  72      -3.130  34.691 -43.539  1.00  0.35
ATOM    307  N   SER A  73      -2.942  34.039 -46.537  1.00  0.45
ATOM    308  CA  SER A  73      -3.557  32.959 -47.308  1.00  0.45
ATOM    309  C   SER A  73      -4.407  33.534 -48.422  1.00  0.45
ATOM    310  O   SER A  73      -4.546  32.952 -49.491  1.00  0.45
ATOM    311  CB  SER A  73      -4.519  32.122 -46.412  1.00  0.45
ATOM    312  OG  SER A  73      -5.458  32.958 -45.717  1.00  0.45
ATOM    313  N   ASN A  74      -4.956  34.736 -48.167  1.00  0.41
ATOM    314  CA  ASN A  74      -5.473  35.688 -49.122  1.00  0.41
ATOM    315  C   ASN A  74      -4.491  36.870 -49.106  1.00  0.41
ATOM    316  O   ASN A  74      -3.287  36.657 -49.005  1.00  0.41
ATOM    317  CB  ASN A  74      -6.923  36.053 -48.676  1.00  0.41
ATOM    318  CG  ASN A  74      -7.757  36.768 -49.737  1.00  0.41
ATOM    319  OD1 ASN A  74      -7.247  37.433 -50.637  1.00  0.41
ATOM    320  ND2 ASN A  74      -9.101  36.694 -49.600  1.00  0.41
ATOM    321  N   ASN A  75      -4.948  38.138 -49.206  1.00  0.54
ATOM    322  CA  ASN A  75      -4.099  39.307 -49.364  1.00  0.54
ATOM    323  C   ASN A  75      -3.560  39.412 -50.780  1.00  0.54
ATOM    324  O   ASN A  75      -2.533  40.064 -50.955  1.00  0.54
ATOM    325  CB  ASN A  75      -2.952  39.441 -48.324  1.00  0.54
ATOM    326  CG  ASN A  75      -3.565  39.593 -46.948  1.00  0.54
ATOM    327  OD1 ASN A  75      -4.227  40.591 -46.669  1.00  0.54
ATOM    328  ND2 ASN A  75      -3.358  38.621 -46.043  1.00  0.54
ATOM    329  N   SER A  76      -4.261  38.796 -51.782  1.00  0.38
ATOM    330  CA  SER A  76      -3.968  38.747 -53.227  1.00  0.38
ATOM    331  C   SER A  76      -2.630  39.319 -53.667  1.00  0.38
ATOM    332  O   SER A  76      -2.517  40.488 -54.045  1.00  0.38
ATOM    333  CB  SER A  76      -5.127  39.285 -54.115  1.00  0.38
ATOM    334  OG  SER A  76      -4.983  38.881 -55.482  1.00  0.38
ATOM    335  N   GLN A  77      -1.570  38.503 -53.568  1.00  0.44
ATOM    336  CA  GLN A  77      -0.218  38.895 -53.868  1.00  0.44
ATOM    337  C   GLN A  77       0.155  38.529 -55.285  1.00  0.44
ATOM    338  O   GLN A  77      -0.036  37.411 -55.746  1.00  0.44
ATOM    339  CB  GLN A  77       0.737  38.179 -52.888  1.00  0.44
ATOM    340  CG  GLN A  77       2.260  38.362 -53.105  1.00  0.44
ATOM    341  CD  GLN A  77       2.730  39.815 -53.144  1.00  0.44
ATOM    342  OE1 GLN A  77       2.512  40.630 -52.244  1.00  0.44
ATOM    343  NE2 GLN A  77       3.441  40.178 -54.238  1.00  0.44
ATOM    344  N   GLN A  78       0.740  39.475 -56.040  1.00  0.50
ATOM    345  CA  GLN A  78       1.293  39.189 -57.346  1.00  0.50
ATOM    346  C   GLN A  78       2.452  38.202 -57.305  1.00  0.50
ATOM    347  O   GLN A  78       3.389  38.352 -56.514  1.00  0.50
ATOM    348  CB  GLN A  78       1.737  40.528 -57.982  1.00  0.50
ATOM    349  CG  GLN A  78       1.769  40.535 -59.525  1.00  0.50
ATOM    350  CD  GLN A  78       2.117  41.929 -60.054  1.00  0.50
ATOM    351  OE1 GLN A  78       2.065  42.937 -59.344  1.00  0.50
ATOM    352  NE2 GLN A  78       2.484  41.992 -61.350  1.00  0.50
ATOM    353  N   GLU A  79       2.428  37.187 -58.191  1.00  0.53
ATOM    354  CA  GLU A  79       3.456  36.188 -58.342  1.00  0.53
ATOM    355  C   GLU A  79       4.657  36.818 -59.006  1.00  0.53
ATOM    356  O   GLU A  79       5.766  36.320 -58.900  1.00  0.53
ATOM    357  CB  GLU A  79       2.946  34.931 -59.108  1.00  0.53
ATOM    358  CG  GLU A  79       2.574  35.107 -60.609  1.00  0.53
ATOM    359  CD  GLU A  79       1.196  35.713 -60.902  1.00  0.53
ATOM    360  OE1 GLU A  79       0.684  36.511 -60.074  1.00  0.53
ATOM    361  OE2 GLU A  79       0.634  35.353 -61.969  1.00  0.53
ATOM    362  N   ASP A  80       4.524  38.000 -59.618  1.00  0.57
ATOM    363  CA  ASP A  80       5.652  38.870 -59.887  1.00  0.57
ATOM    364  C   ASP A  80       6.135  39.583 -58.609  1.00  0.57
ATOM    365  O   ASP A  80       5.962  40.791 -58.441  1.00  0.57
ATOM    366  CB  ASP A  80       5.338  39.919 -60.981  1.00  0.57
ATOM    367  CG  ASP A  80       4.617  39.288 -62.155  1.00  0.57
ATOM    368  OD1 ASP A  80       5.231  38.450 -62.856  1.00  0.57
ATOM    369  OD2 ASP A  80       3.438  39.677 -62.368  1.00  0.57
ATOM    370  N   PHE A  81       6.746  38.851 -57.645  1.00  0.47
ATOM    371  CA  PHE A  81       7.432  39.405 -56.484  1.00  0.47
ATOM    372  C   PHE A  81       8.350  40.599 -56.825  1.00  0.47
ATOM    373  O   PHE A  81       8.993  40.661 -57.868  1.00  0.47
ATOM    374  CB  PHE A  81       8.138  38.277 -55.668  1.00  0.47
ATOM    375  CG  PHE A  81       9.033  38.762 -54.568  1.00  0.47
ATOM    376  CD1 PHE A  81       8.535  39.594 -53.557  1.00  0.47
ATOM    377  CD2 PHE A  81      10.403  38.460 -54.599  1.00  0.47
ATOM    378  CE1 PHE A  81       9.415  40.186 -52.645  1.00  0.47
ATOM    379  CE2 PHE A  81      11.274  39.016 -53.656  1.00  0.47
ATOM    380  CZ  PHE A  81      10.777  39.888 -52.683  1.00  0.47
ATOM    381  N   ARG A  82       8.394  41.615 -55.940  1.00  0.59
ATOM    382  CA  ARG A  82       9.269  42.764 -56.056  1.00  0.59
ATOM    383  C   ARG A  82      10.760  42.464 -56.101  1.00  0.59
ATOM    384  O   ARG A  82      11.251  41.441 -55.637  1.00  0.59
ATOM    385  CB  ARG A  82       9.041  43.759 -54.899  1.00  0.59
ATOM    386  CG  ARG A  82       7.594  44.272 -54.792  1.00  0.59
ATOM    387  CD  ARG A  82       7.429  45.309 -53.677  1.00  0.59
ATOM    388  NE  ARG A  82       5.995  45.747 -53.685  1.00  0.59
ATOM    389  CZ  ARG A  82       5.512  46.649 -52.819  1.00  0.59
ATOM    390  NH1 ARG A  82       4.256  47.076 -52.950  1.00  0.59
ATOM    391  NH2 ARG A  82       6.264  47.130 -51.834  1.00  0.59
ATOM    392  N   SER A  83      11.549  43.385 -56.671  1.00  0.75
ATOM    393  CA  SER A  83      12.979  43.221 -56.807  1.00  0.75
ATOM    394  C   SER A  83      13.721  43.621 -55.539  1.00  0.75
ATOM    395  O   SER A  83      13.691  44.765 -55.092  1.00  0.75
ATOM    396  CB  SER A  83      13.515  44.017 -58.027  1.00  0.75
ATOM    397  OG  SER A  83      12.998  45.352 -58.055  1.00  0.75
ATOM    398  N   VAL A  84      14.416  42.654 -54.909  1.00  0.78
ATOM    399  CA  VAL A  84      15.207  42.893 -53.711  1.00  0.78
ATOM    400  C   VAL A  84      16.571  42.296 -53.955  1.00  0.78
ATOM    401  O   VAL A  84      16.686  41.100 -54.202  1.00  0.78
ATOM    402  CB  VAL A  84      14.626  42.281 -52.434  1.00  0.78
ATOM    403  CG1 VAL A  84      15.371  42.826 -51.203  1.00  0.78
ATOM    404  CG2 VAL A  84      13.128  42.603 -52.314  1.00  0.78
ATOM    405  N   SER A  85      17.635  43.120 -53.904  1.00  0.83
ATOM    406  CA  SER A  85      18.977  42.704 -54.288  1.00  0.83
ATOM    407  C   SER A  85      19.955  42.898 -53.156  1.00  0.83
ATOM    408  O   SER A  85      20.137  44.011 -52.665  1.00  0.83
ATOM    409  CB  SER A  85      19.566  43.531 -55.465  1.00  0.83
ATOM    410  OG  SER A  85      18.739  43.463 -56.624  1.00  0.83
ATOM    411  N   PHE A  86      20.655  41.829 -52.727  1.00  0.85
ATOM    412  CA  PHE A  86      21.609  41.883 -51.630  1.00  0.85
ATOM    413  C   PHE A  86      23.036  41.550 -52.072  1.00  0.85
ATOM    414  O   PHE A  86      23.528  40.464 -51.760  1.00  0.85
ATOM    415  CB  PHE A  86      21.222  40.896 -50.496  1.00  0.85
ATOM    416  CG  PHE A  86      19.844  41.168 -49.975  1.00  0.85
ATOM    417  CD1 PHE A  86      19.586  42.309 -49.203  1.00  0.85
ATOM    418  CD2 PHE A  86      18.800  40.265 -50.227  1.00  0.85
ATOM    419  CE1 PHE A  86      18.303  42.555 -48.700  1.00  0.85
ATOM    420  CE2 PHE A  86      17.517  40.500 -49.726  1.00  0.85
ATOM    421  CZ  PHE A  86      17.275  41.646 -48.960  1.00  0.85
ATOM    422  N   PRO A  87      23.788  42.411 -52.763  1.00  0.86
ATOM    423  CA  PRO A  87      25.157  42.108 -53.185  1.00  0.86
ATOM    424  C   PRO A  87      26.153  42.151 -52.040  1.00  0.86
ATOM    425  O   PRO A  87      27.322  41.839 -52.245  1.00  0.86
ATOM    426  CB  PRO A  87      25.449  43.209 -54.215  1.00  0.86
ATOM    427  CG  PRO A  87      24.641  44.408 -53.711  1.00  0.86
ATOM    428  CD  PRO A  87      23.363  43.748 -53.195  1.00  0.86
ATOM    429  N   LYS A  88      25.731  42.562 -50.833  1.00  0.85
ATOM    430  CA  LYS A  88      26.551  42.549 -49.641  1.00  0.85
ATOM    431  C   LYS A  88      26.936  41.141 -49.201  1.00  0.85
ATOM    432  O   LYS A  88      28.082  40.899 -48.835  1.00  0.85
ATOM    433  CB  LYS A  88      25.792  43.231 -48.472  1.00  0.85
ATOM    434  CG  LYS A  88      25.168  44.608 -48.777  1.00  0.85
ATOM    435  CD  LYS A  88      26.149  45.796 -48.779  1.00  0.85
ATOM    436  CE  LYS A  88      25.416  47.133 -48.983  1.00  0.85
ATOM    437  NZ  LYS A  88      26.327  48.289 -48.803  1.00  0.85
ATOM    438  N   LEU A  89      25.972  40.192 -49.225  1.00  0.88
ATOM    439  CA  LEU A  89      26.134  38.846 -48.706  1.00  0.88
ATOM    440  C   LEU A  89      27.063  37.971 -49.527  1.00  0.88
ATOM    441  O   LEU A  89      26.840  37.730 -50.713  1.00  0.88
ATOM    442  CB  LEU A  89      24.757  38.143 -48.551  1.00  0.88
ATOM    443  CG  LEU A  89      24.803  36.715 -47.950  1.00  0.88
ATOM    444  CD1 LEU A  89      25.522  36.680 -46.596  1.00  0.88
ATOM    445  CD2 LEU A  89      23.403  36.104 -47.792  1.00  0.88
ATOM    446  N   THR A  90      28.124  37.448 -48.879  1.00  0.89
ATOM    447  CA  THR A  90      29.112  36.595 -49.524  1.00  0.89
ATOM    448  C   THR A  90      29.307  35.268 -48.813  1.00  0.89
ATOM    449  O   THR A  90      29.643  34.270 -49.459  1.00  0.89
ATOM    450  CB  THR A  90      30.479  37.268 -49.618  1.00  0.89
ATOM    451  OG1 THR A  90      30.935  37.690 -48.342  1.00  0.89
ATOM    452  CG2 THR A  90      30.370  38.523 -50.493  1.00  0.89
ATOM    453  N   VAL A  91      29.088  35.195 -47.480  1.00  0.89
ATOM    454  CA  VAL A  91      29.375  33.999 -46.693  1.00  0.89
ATOM    455  C   VAL A  91      28.208  33.626 -45.785  1.00  0.89
ATOM    456  O   VAL A  91      27.685  34.449 -45.034  1.00  0.89
ATOM    457  CB  VAL A  91      30.637  34.132 -45.827  1.00  0.89
ATOM    458  CG1 VAL A  91      31.026  32.769 -45.208  1.00  0.89
ATOM    459  CG2 VAL A  91      31.812  34.658 -46.673  1.00  0.89
ATOM    460  N   ILE A  92      27.785  32.343 -45.807  1.00  0.89
ATOM    461  CA  ILE A  92      26.849  31.778 -44.836  1.00  0.89
ATOM    462  C   ILE A  92      27.589  30.709 -44.035  1.00  0.89
ATOM    463  O   ILE A  92      28.256  29.837 -44.593  1.00  0.89
ATOM    464  CB  ILE A  92      25.583  31.233 -45.511  1.00  0.89
ATOM    465  CG1 ILE A  92      24.799  32.423 -46.129  1.00  0.89
ATOM    466  CG2 ILE A  92      24.715  30.441 -44.502  1.00  0.89
ATOM    467  CD1 ILE A  92      23.480  32.058 -46.825  1.00  0.89
ATOM    468  N   THR A  93      27.567  30.774 -42.681  1.00  0.87
ATOM    469  CA  THR A  93      28.358  29.862 -41.847  1.00  0.87
ATOM    470  C   THR A  93      27.729  28.494 -41.707  1.00  0.87
ATOM    471  O   THR A  93      28.422  27.478 -41.737  1.00  0.87
ATOM    472  CB  THR A  93      28.774  30.390 -40.467  1.00  0.87
ATOM    473  OG1 THR A  93      27.716  30.418 -39.523  1.00  0.87
ATOM    474  CG2 THR A  93      29.306  31.820 -40.620  1.00  0.87
ATOM    475  N   GLY A  94      26.396  28.425 -41.550  1.00  0.88
ATOM    476  CA  GLY A  94      25.633  27.192 -41.489  1.00  0.88
ATOM    477  C   GLY A  94      25.064  26.830 -42.826  1.00  0.88
ATOM    478  O   GLY A  94      25.726  26.918 -43.857  1.00  0.88
ATOM    479  N   TYR A  95      23.802  26.376 -42.826  1.00  0.86
ATOM    480  CA  TYR A  95      23.077  25.984 -44.014  1.00  0.86
ATOM    481  C   TYR A  95      22.127  27.069 -44.527  1.00  0.86
ATOM    482  O   TYR A  95      21.715  27.978 -43.804  1.00  0.86
ATOM    483  CB  TYR A  95      22.291  24.663 -43.765  1.00  0.86
ATOM    484  CG  TYR A  95      21.266  24.799 -42.667  1.00  0.86
ATOM    485  CD1 TYR A  95      19.976  25.250 -42.981  1.00  0.86
ATOM    486  CD2 TYR A  95      21.559  24.467 -41.334  1.00  0.86
ATOM    487  CE1 TYR A  95      18.995  25.361 -41.990  1.00  0.86
ATOM    488  CE2 TYR A  95      20.572  24.558 -40.340  1.00  0.86
ATOM    489  CZ  TYR A  95      19.288  25.012 -40.666  1.00  0.86
ATOM    490  OH  TYR A  95      18.301  25.120 -39.661  1.00  0.86
ATOM    491  N   LEU A  96      21.719  26.949 -45.804  1.00  0.89
ATOM    492  CA  LEU A  96      20.721  27.800 -46.429  1.00  0.89
ATOM    493  C   LEU A  96      19.495  26.973 -46.808  1.00  0.89
ATOM    494  O   LEU A  96      19.596  25.929 -47.452  1.00  0.89
ATOM    495  CB  LEU A  96      21.344  28.486 -47.673  1.00  0.89
ATOM    496  CG  LEU A  96      20.396  29.299 -48.586  1.00  0.89
ATOM    497  CD1 LEU A  96      19.594  30.368 -47.830  1.00  0.89
ATOM    498  CD2 LEU A  96      21.201  29.966 -49.714  1.00  0.89
ATOM    499  N   LEU A  97      18.289  27.412 -46.384  1.00  0.89
ATOM    500  CA  LEU A  97      17.044  26.703 -46.637  1.00  0.89
ATOM    501  C   LEU A  97      16.035  27.613 -47.319  1.00  0.89
ATOM    502  O   LEU A  97      15.642  28.652 -46.784  1.00  0.89
ATOM    503  CB  LEU A  97      16.453  26.168 -45.306  1.00  0.89
ATOM    504  CG  LEU A  97      15.541  24.920 -45.393  1.00  0.89
ATOM    505  CD1 LEU A  97      15.389  24.287 -44.003  1.00  0.89
ATOM    506  CD2 LEU A  97      14.151  25.166 -45.999  1.00  0.89
ATOM    507  N   LEU A  98      15.580  27.214 -48.521  1.00  0.89
ATOM    508  CA  LEU A  98      14.589  27.918 -49.310  1.00  0.89
ATOM    509  C   LEU A  98      13.363  27.034 -49.472  1.00  0.89
ATOM    510  O   LEU A  98      13.451  25.925 -50.000  1.00  0.89
ATOM    511  CB  LEU A  98      15.161  28.236 -50.712  1.00  0.89
ATOM    512  CG  LEU A  98      16.301  29.270 -50.687  1.00  0.89
ATOM    513  CD1 LEU A  98      17.263  29.034 -51.848  1.00  0.89
ATOM    514  CD2 LEU A  98      15.770  30.705 -50.746  1.00  0.89
ATOM    515  N   PHE A  99      12.185  27.492 -48.996  1.00  0.87
ATOM    516  CA  PHE A  99      10.973  26.692 -49.047  1.00  0.87
ATOM    517  C   PHE A  99       9.759  27.534 -49.421  1.00  0.87
ATOM    518  O   PHE A  99       9.420  28.506 -48.749  1.00  0.87
ATOM    519  CB  PHE A  99      10.790  25.954 -47.690  1.00  0.87
ATOM    520  CG  PHE A  99       9.555  25.100 -47.592  1.00  0.87
ATOM    521  CD1 PHE A  99       9.408  23.932 -48.357  1.00  0.87
ATOM    522  CD2 PHE A  99       8.541  25.449 -46.687  1.00  0.87
ATOM    523  CE1 PHE A  99       8.264  23.133 -48.227  1.00  0.87
ATOM    524  CE2 PHE A  99       7.400  24.651 -46.547  1.00  0.87
ATOM    525  CZ  PHE A  99       7.259  23.494 -47.322  1.00  0.87
ATOM    526  N   ARG A 100       9.059  27.170 -50.519  1.00  0.81
ATOM    527  CA  ARG A 100       7.808  27.784 -50.954  1.00  0.81
ATOM    528  C   ARG A 100       7.783  29.300 -51.064  1.00  0.81
ATOM    529  O   ARG A 100       6.882  29.978 -50.570  1.00  0.81
ATOM    530  CB  ARG A 100       6.592  27.287 -50.149  1.00  0.81
ATOM    531  CG  ARG A 100       6.475  25.755 -50.161  1.00  0.81
ATOM    532  CD  ARG A 100       5.106  25.221 -49.746  1.00  0.81
ATOM    533  NE  ARG A 100       4.193  25.520 -50.892  1.00  0.81
ATOM    534  CZ  ARG A 100       2.901  25.179 -50.929  1.00  0.81
ATOM    535  NH1 ARG A 100       2.298  24.617 -49.889  1.00  0.81
ATOM    536  NH2 ARG A 100       2.203  25.433 -52.034  1.00  0.81
ATOM    537  N   VAL A 101       8.780  29.862 -51.755  1.00  0.77
ATOM    538  CA  VAL A 101       8.864  31.276 -52.054  1.00  0.77
ATOM    539  C   VAL A 101       8.285  31.479 -53.427  1.00  0.77
ATOM    540  O   VAL A 101       8.755  30.900 -54.402  1.00  0.77
ATOM    541  CB  VAL A 101      10.305  31.750 -52.061  1.00  0.77
ATOM    542  CG1 VAL A 101      10.465  33.245 -52.416  1.00  0.77
ATOM    543  CG2 VAL A 101      10.941  31.426 -50.699  1.00  0.77
ATOM    544  N   SER A 102       7.225  32.286 -53.539  1.00  0.73
ATOM    545  CA  SER A 102       6.545  32.507 -54.798  1.00  0.73
ATOM    546  C   SER A 102       7.032  33.772 -55.430  1.00  0.73
ATOM    547  O   SER A 102       7.226  34.791 -54.769  1.00  0.73
ATOM    548  CB  SER A 102       5.017  32.614 -54.641  1.00  0.73
ATOM    549  OG  SER A 102       4.326  32.673 -55.889  1.00  0.73
ATOM    550  N   GLY A 103       7.262  33.731 -56.750  1.00  0.75
ATOM    551  CA  GLY A 103       7.700  34.907 -57.468  1.00  0.75
ATOM    552  C   GLY A 103       9.151  35.220 -57.392  1.00  0.75
ATOM    553  O   GLY A 103       9.613  36.264 -57.839  1.00  0.75
ATOM    554  N   LEU A 104       9.951  34.310 -56.848  1.00  0.77
ATOM    555  CA  LEU A 104      11.380  34.375 -57.016  1.00  0.77
ATOM    556  C   LEU A 104      11.785  33.530 -58.212  1.00  0.77
ATOM    557  O   LEU A 104      11.792  32.305 -58.129  1.00  0.77
ATOM    558  CB  LEU A 104      12.109  33.877 -55.745  1.00  0.77
ATOM    559  CG  LEU A 104      13.646  33.963 -55.817  1.00  0.77
ATOM    560  CD1 LEU A 104      14.117  35.417 -55.958  1.00  0.77
ATOM    561  CD2 LEU A 104      14.285  33.300 -54.590  1.00  0.77
ATOM    562  N   ASP A 105      12.130  34.145 -59.367  1.00  0.83
ATOM    563  CA  ASP A 105      12.569  33.401 -60.538  1.00  0.83
ATOM    564  C   ASP A 105      13.973  32.802 -60.447  1.00  0.83
ATOM    565  O   ASP A 105      14.265  31.769 -61.038  1.00  0.83
ATOM    566  CB  ASP A 105      12.582  34.256 -61.824  1.00  0.83
ATOM    567  CG  ASP A 105      11.212  34.736 -62.249  1.00  0.83
ATOM    568  OD1 ASP A 105      10.343  33.897 -62.570  1.00  0.83
ATOM    569  OD2 ASP A 105      11.064  35.972 -62.375  1.00  0.83
ATOM    570  N   SER A 106      14.910  33.440 -59.731  1.00  0.85
ATOM    571  CA  SER A 106      16.278  32.962 -59.690  1.00  0.85
ATOM    572  C   SER A 106      16.931  33.423 -58.409  1.00  0.85
ATOM    573  O   SER A 106      16.624  34.489 -57.885  1.00  0.85
ATOM    574  CB  SER A 106      17.145  33.457 -60.868  1.00  0.85
ATOM    575  OG  SER A 106      18.485  33.017 -60.696  1.00  0.85
ATOM    576  N   LEU A 107      17.906  32.650 -57.883  1.00  0.85
ATOM    577  CA  LEU A 107      18.642  33.029 -56.690  1.00  0.85
ATOM    578  C   LEU A 107      19.649  34.156 -56.912  1.00  0.85
ATOM    579  O   LEU A 107      20.112  34.764 -55.947  1.00  0.85
ATOM    580  CB  LEU A 107      19.368  31.828 -56.025  1.00  0.85
ATOM    581  CG  LEU A 107      18.479  30.635 -55.596  1.00  0.85
ATOM    582  CD1 LEU A 107      19.288  29.655 -54.727  1.00  0.85
ATOM    583  CD2 LEU A 107      17.208  31.063 -54.844  1.00  0.85
ATOM    584  N   SER A 108      19.982  34.510 -58.174  1.00  0.83
ATOM    585  CA  SER A 108      20.855  35.644 -58.477  1.00  0.83
ATOM    586  C   SER A 108      20.240  36.981 -58.146  1.00  0.83
ATOM    587  O   SER A 108      20.938  37.951 -57.867  1.00  0.83
ATOM    588  CB  SER A 108      21.239  35.718 -59.978  1.00  0.83
ATOM    589  OG  SER A 108      20.102  35.853 -60.834  1.00  0.83
ATOM    590  N   VAL A 109      18.896  37.042 -58.171  1.00  0.81
ATOM    591  CA  VAL A 109      18.112  38.213 -57.848  1.00  0.81
ATOM    592  C   VAL A 109      18.360  38.653 -56.421  1.00  0.81
ATOM    593  O   VAL A 109      18.563  39.831 -56.149  1.00  0.81
ATOM    594  CB  VAL A 109      16.631  37.910 -58.061  1.00  0.81
ATOM    595  CG1 VAL A 109      15.746  39.116 -57.689  1.00  0.81
ATOM    596  CG2 VAL A 109      16.396  37.509 -59.533  1.00  0.81
ATOM    597  N   LEU A 110      18.406  37.693 -55.476  1.00  0.84
ATOM    598  CA  LEU A 110      18.644  38.001 -54.085  1.00  0.84
ATOM    599  C   LEU A 110      20.117  38.041 -53.712  1.00  0.84
ATOM    600  O   LEU A 110      20.587  39.041 -53.177  1.00  0.84
ATOM    601  CB  LEU A 110      17.947  36.966 -53.172  1.00  0.84
ATOM    602  CG  LEU A 110      16.438  36.786 -53.434  1.00  0.84
ATOM    603  CD1 LEU A 110      15.858  35.736 -52.478  1.00  0.84
ATOM    604  CD2 LEU A 110      15.649  38.098 -53.321  1.00  0.84
ATOM    605  N   PHE A 111      20.898  36.971 -53.986  1.00  0.86
ATOM    606  CA  PHE A 111      22.259  36.853 -53.468  1.00  0.86
ATOM    607  C   PHE A 111      23.257  36.629 -54.588  1.00  0.86
ATOM    608  O   PHE A 111      23.721  35.502 -54.778  1.00  0.86
ATOM    609  CB  PHE A 111      22.425  35.688 -52.450  1.00  0.86
ATOM    610  CG  PHE A 111      21.330  35.711 -51.431  1.00  0.86
ATOM    611  CD1 PHE A 111      21.194  36.794 -50.552  1.00  0.86
ATOM    612  CD2 PHE A 111      20.394  34.666 -51.384  1.00  0.86
ATOM    613  CE1 PHE A 111      20.121  36.850 -49.658  1.00  0.86
ATOM    614  CE2 PHE A 111      19.313  34.722 -50.496  1.00  0.86
ATOM    615  CZ  PHE A 111      19.172  35.822 -49.640  1.00  0.86
ATOM    616  N   PRO A 112      23.660  37.631 -55.357  1.00  0.85
ATOM    617  CA  PRO A 112      24.504  37.405 -56.519  1.00  0.85
ATOM    618  C   PRO A 112      25.933  37.137 -56.106  1.00  0.85
ATOM    619  O   PRO A 112      26.661  36.484 -56.846  1.00  0.85
ATOM    620  CB  PRO A 112      24.362  38.712 -57.312  1.00  0.85
ATOM    621  CG  PRO A 112      24.077  39.780 -56.252  1.00  0.85
ATOM    622  CD  PRO A 112      23.209  39.023 -55.248  1.00  0.85
ATOM    623  N   ASN A 113      26.358  37.629 -54.930  1.00  0.85
ATOM    624  CA  ASN A 113      27.736  37.573 -54.494  1.00  0.85
ATOM    625  C   ASN A 113      27.981  36.457 -53.485  1.00  0.85
ATOM    626  O   ASN A 113      29.073  36.364 -52.928  1.00  0.85
ATOM    627  CB  ASN A 113      28.170  38.932 -53.882  1.00  0.85
ATOM    628  CG  ASN A 113      28.244  40.030 -54.941  1.00  0.85
ATOM    629  OD1 ASN A 113      27.709  39.959 -56.047  1.00  0.85
ATOM    630  ND2 ASN A 113      28.967  41.120 -54.604  1.00  0.85
ATOM    631  N   LEU A 114      26.994  35.564 -53.238  1.00  0.87
ATOM    632  CA  LEU A 114      27.149  34.428 -52.340  1.00  0.87
ATOM    633  C   LEU A 114      28.188  33.428 -52.834  1.00  0.87
ATOM    634  O   LEU A 114      28.003  32.763 -53.850  1.00  0.87
ATOM    635  CB  LEU A 114      25.788  33.728 -52.097  1.00  0.87
ATOM    636  CG  LEU A 114      25.788  32.521 -51.127  1.00  0.87
ATOM    637  CD1 LEU A 114      26.309  32.881 -49.727  1.00  0.87
ATOM    638  CD2 LEU A 114      24.374  31.931 -51.004  1.00  0.87
ATOM    639  N   SER A 115      29.321  33.317 -52.111  1.00  0.86
ATOM    640  CA  SER A 115      30.499  32.621 -52.604  1.00  0.86
ATOM    641  C   SER A 115      30.773  31.356 -51.827  1.00  0.86
ATOM    642  O   SER A 115      31.192  30.347 -52.398  1.00  0.86
ATOM    643  CB  SER A 115      31.780  33.499 -52.483  1.00  0.86
ATOM    644  OG  SER A 115      31.791  34.560 -53.436  1.00  0.86
ATOM    645  N   VAL A 116      30.542  31.359 -50.499  1.00  0.88
ATOM    646  CA  VAL A 116      30.876  30.228 -49.649  1.00  0.88
ATOM    647  C   VAL A 116      29.718  29.937 -48.714  1.00  0.88
ATOM    648  O   VAL A 116      29.263  30.797 -47.957  1.00  0.88
ATOM    649  CB  VAL A 116      32.180  30.412 -48.859  1.00  0.88
ATOM    650  CG1 VAL A 116      32.467  29.178 -47.975  1.00  0.88
ATOM    651  CG2 VAL A 116      33.359  30.589 -49.839  1.00  0.88
ATOM    652  N   ILE A 117      29.220  28.685 -48.730  1.00  0.87
ATOM    653  CA  ILE A 117      28.308  28.187 -47.709  1.00  0.87
ATOM    654  C   ILE A 117      29.101  27.187 -46.901  1.00  0.87
ATOM    655  O   ILE A 117      29.418  26.091 -47.353  1.00  0.87
ATOM    656  CB  ILE A 117      27.044  27.538 -48.272  1.00  0.87
ATOM    657  CG1 ILE A 117      26.224  28.596 -49.051  1.00  0.87
ATOM    658  CG2 ILE A 117      26.213  26.919 -47.121  1.00  0.87
ATOM    659  CD1 ILE A 117      24.905  28.069 -49.636  1.00  0.87
ATOM    660  N   ARG A 118      29.487  27.541 -45.663  1.00  0.82
ATOM    661  CA  ARG A 118      30.420  26.712 -44.928  1.00  0.82
ATOM    662  C   ARG A 118      29.778  25.488 -44.313  1.00  0.82
ATOM    663  O   ARG A 118      30.443  24.486 -44.065  1.00  0.82
ATOM    664  CB  ARG A 118      31.134  27.496 -43.806  1.00  0.82
ATOM    665  CG  ARG A 118      31.937  28.708 -44.305  1.00  0.82
ATOM    666  CD  ARG A 118      32.641  29.463 -43.175  1.00  0.82
ATOM    667  NE  ARG A 118      33.702  28.576 -42.572  1.00  0.82
ATOM    668  CZ  ARG A 118      35.015  28.682 -42.827  1.00  0.82
ATOM    669  NH1 ARG A 118      35.445  29.424 -43.832  1.00  0.82
ATOM    670  NH2 ARG A 118      35.879  28.079 -42.016  1.00  0.82
ATOM    671  N   GLY A 119      28.456  25.511 -44.055  1.00  0.86
ATOM    672  CA  GLY A 119      27.761  24.343 -43.540  1.00  0.86
ATOM    673  C   GLY A 119      28.239  23.835 -42.207  1.00  0.86
ATOM    674  O   GLY A 119      28.229  22.634 -41.980  1.00  0.86
ATOM    675  N   HIS A 120      28.692  24.715 -41.287  1.00  0.80
ATOM    676  CA  HIS A 120      29.293  24.330 -40.013  1.00  0.80
ATOM    677  C   HIS A 120      28.369  23.459 -39.188  1.00  0.80
ATOM    678  O   HIS A 120      28.749  22.400 -38.690  1.00  0.80
ATOM    679  CB  HIS A 120      29.627  25.597 -39.194  1.00  0.80
ATOM    680  CG  HIS A 120      30.272  25.326 -37.873  1.00  0.80
ATOM    681  ND1 HIS A 120      31.528  24.757 -37.858  1.00  0.80
ATOM    682  CD2 HIS A 120      29.836  25.558 -36.607  1.00  0.80
ATOM    683  CE1 HIS A 120      31.836  24.657 -36.578  1.00  0.80
ATOM    684  NE2 HIS A 120      30.846  25.124 -35.781  1.00  0.80
ATOM    685  N   ASN A 121      27.090  23.857 -39.146  1.00  0.80
ATOM    686  CA  ASN A 121      26.000  23.028 -38.696  1.00  0.80
ATOM    687  C   ASN A 121      25.081  22.813 -39.886  1.00  0.80
ATOM    688  O   ASN A 121      24.919  23.702 -40.722  1.00  0.80
ATOM    689  CB  ASN A 121      25.212  23.698 -37.548  1.00  0.80
ATOM    690  CG  ASN A 121      26.107  23.812 -36.321  1.00  0.80
ATOM    691  OD1 ASN A 121      26.601  22.805 -35.812  1.00  0.80
ATOM    692  ND2 ASN A 121      26.310  25.050 -35.815  1.00  0.80
ATOM    693  N   LEU A 122      24.478  21.614 -40.006  1.00  0.81
ATOM    694  CA  LEU A 122      23.776  21.200 -41.203  1.00  0.81
ATOM    695  C   LEU A 122      22.317  20.971 -40.913  1.00  0.81
ATOM    696  O   LEU A 122      21.925  20.573 -39.818  1.00  0.81
ATOM    697  CB  LEU A 122      24.339  19.883 -41.796  1.00  0.81
ATOM    698  CG  LEU A 122      25.810  19.959 -42.238  1.00  0.81
ATOM    699  CD1 LEU A 122      26.289  18.578 -42.707  1.00  0.81
ATOM    700  CD2 LEU A 122      26.009  20.997 -43.352  1.00  0.81
ATOM    701  N   PHE A 123      21.457  21.192 -41.919  1.00  0.85
ATOM    702  CA  PHE A 123      20.066  20.818 -41.824  1.00  0.85
ATOM    703  C   PHE A 123      19.940  19.403 -42.332  1.00  0.85
ATOM    704  O   PHE A 123      19.868  19.166 -43.534  1.00  0.85
ATOM    705  CB  PHE A 123      19.180  21.791 -42.638  1.00  0.85
ATOM    706  CG  PHE A 123      17.707  21.561 -42.449  1.00  0.85
ATOM    707  CD1 PHE A 123      17.049  22.016 -41.295  1.00  0.85
ATOM    708  CD2 PHE A 123      16.964  20.917 -43.449  1.00  0.85
ATOM    709  CE1 PHE A 123      15.670  21.830 -41.145  1.00  0.85
ATOM    710  CE2 PHE A 123      15.585  20.728 -43.305  1.00  0.85
ATOM    711  CZ  PHE A 123      14.942  21.188 -42.151  1.00  0.85
ATOM    712  N   TYR A 124      19.962  18.411 -41.418  1.00  0.79
ATOM    713  CA  TYR A 124      19.712  17.021 -41.764  1.00  0.79
ATOM    714  C   TYR A 124      20.750  16.451 -42.754  1.00  0.79
ATOM    715  O   TYR A 124      20.436  15.672 -43.649  1.00  0.79
ATOM    716  CB  TYR A 124      18.239  16.899 -42.282  1.00  0.79
ATOM    717  CG  TYR A 124      17.611  15.540 -42.320  1.00  0.79
ATOM    718  CD1 TYR A 124      18.284  14.391 -41.884  1.00  0.79
ATOM    719  CD2 TYR A 124      16.370  15.386 -42.970  1.00  0.79
ATOM    720  CE1 TYR A 124      17.781  13.135 -42.173  1.00  0.79
ATOM    721  CE2 TYR A 124      15.874  14.133 -43.280  1.00  0.79
ATOM    722  CZ  TYR A 124      16.592  13.061 -42.859  1.00  0.79
ATOM    723  OH  TYR A 124      16.095  11.813 -43.150  1.00  0.79
ATOM    724  N   ASN A 125      22.028  16.863 -42.591  1.00  0.79
ATOM    725  CA  ASN A 125      23.189  16.530 -43.416  1.00  0.79
ATOM    726  C   ASN A 125      23.282  17.328 -44.712  1.00  0.79
ATOM    727  O   ASN A 125      24.202  17.141 -45.511  1.00  0.79
ATOM    728  CB  ASN A 125      23.411  15.012 -43.654  1.00  0.79
ATOM    729  CG  ASN A 125      23.487  14.327 -42.298  1.00  0.79
ATOM    730  OD1 ASN A 125      24.028  14.873 -41.334  1.00  0.79
ATOM    731  ND2 ASN A 125      22.947  13.093 -42.199  1.00  0.79
ATOM    732  N   TYR A 126      22.393  18.320 -44.902  1.00  0.82
ATOM    733  CA  TYR A 126      22.393  19.180 -46.064  1.00  0.82
ATOM    734  C   TYR A 126      22.825  20.602 -45.717  1.00  0.82
ATOM    735  O   TYR A 126      22.476  21.167 -44.679  1.00  0.82
ATOM    736  CB  TYR A 126      21.000  19.248 -46.741  1.00  0.82
ATOM    737  CG  TYR A 126      20.514  17.873 -47.133  1.00  0.82
ATOM    738  CD1 TYR A 126      21.066  17.187 -48.228  1.00  0.82
ATOM    739  CD2 TYR A 126      19.490  17.249 -46.404  1.00  0.82
ATOM    740  CE1 TYR A 126      20.590  15.918 -48.599  1.00  0.82
ATOM    741  CE2 TYR A 126      19.024  15.975 -46.758  1.00  0.82
ATOM    742  CZ  TYR A 126      19.558  15.314 -47.868  1.00  0.82
ATOM    743  OH  TYR A 126      19.033  14.050 -48.227  1.00  0.82
ATOM    744  N   ALA A 127      23.625  21.219 -46.608  1.00  0.88
ATOM    745  CA  ALA A 127      24.097  22.582 -46.468  1.00  0.88
ATOM    746  C   ALA A 127      23.281  23.556 -47.304  1.00  0.88
ATOM    747  O   ALA A 127      23.227  24.755 -47.030  1.00  0.88
ATOM    748  CB  ALA A 127      25.561  22.638 -46.936  1.00  0.88
ATOM    749  N   LEU A 128      22.575  23.044 -48.321  1.00  0.89
ATOM    750  CA  LEU A 128      21.664  23.821 -49.123  1.00  0.89
ATOM    751  C   LEU A 128      20.446  22.973 -49.416  1.00  0.89
ATOM    752  O   LEU A 128      20.549  21.836 -49.880  1.00  0.89
ATOM    753  CB  LEU A 128      22.354  24.293 -50.425  1.00  0.89
ATOM    754  CG  LEU A 128      21.474  25.057 -51.441  1.00  0.89
ATOM    755  CD1 LEU A 128      20.826  26.317 -50.849  1.00  0.89
ATOM    756  CD2 LEU A 128      22.322  25.449 -52.660  1.00  0.89
ATOM    757  N   VAL A 129      19.254  23.519 -49.119  1.00  0.89
ATOM    758  CA  VAL A 129      17.981  22.889 -49.406  1.00  0.89
ATOM    759  C   VAL A 129      17.156  23.859 -50.225  1.00  0.89
ATOM    760  O   VAL A 129      16.866  24.976 -49.794  1.00  0.89
ATOM    761  CB  VAL A 129      17.213  22.495 -48.151  1.00  0.89
ATOM    762  CG1 VAL A 129      15.817  21.922 -48.489  1.00  0.89
ATOM    763  CG2 VAL A 129      18.036  21.457 -47.361  1.00  0.89
ATOM    764  N   ILE A 130      16.752  23.445 -51.441  1.00  0.89
ATOM    765  CA  ILE A 130      15.837  24.194 -52.288  1.00  0.89
ATOM    766  C   ILE A 130      14.643  23.293 -52.517  1.00  0.89
ATOM    767  O   ILE A 130      14.712  22.333 -53.284  1.00  0.89
ATOM    768  CB  ILE A 130      16.480  24.586 -53.624  1.00  0.89
ATOM    769  CG1 ILE A 130      17.720  25.476 -53.359  1.00  0.89
ATOM    770  CG2 ILE A 130      15.465  25.302 -54.546  1.00  0.89
ATOM    771  CD1 ILE A 130      18.466  25.925 -54.620  1.00  0.89
ATOM    772  N   TYR A 131      13.512  23.568 -51.835  1.00  0.89
ATOM    773  CA  TYR A 131      12.407  22.627 -51.794  1.00  0.89
ATOM    774  C   TYR A 131      11.075  23.312 -52.018  1.00  0.89
ATOM    775  O   TYR A 131      10.755  24.315 -51.385  1.00  0.89
ATOM    776  CB  TYR A 131      12.408  21.858 -50.439  1.00  0.89
ATOM    777  CG  TYR A 131      11.478  20.664 -50.375  1.00  0.89
ATOM    778  CD1 TYR A 131      11.240  19.854 -51.491  1.00  0.89
ATOM    779  CD2 TYR A 131      10.890  20.289 -49.158  1.00  0.89
ATOM    780  CE1 TYR A 131      10.439  18.718 -51.414  1.00  0.89
ATOM    781  CE2 TYR A 131      10.139  19.109 -49.052  1.00  0.89
ATOM    782  CZ  TYR A 131       9.909  18.333 -50.195  1.00  0.89
ATOM    783  OH  TYR A 131       9.180  17.145 -50.197  1.00  0.89
ATOM    784  N   GLU A 132      10.275  22.789 -52.968  1.00  0.84
ATOM    785  CA  GLU A 132       8.957  23.303 -53.321  1.00  0.84
ATOM    786  C   GLU A 132       8.971  24.777 -53.720  1.00  0.84
ATOM    787  O   GLU A 132       8.082  25.569 -53.399  1.00  0.84
ATOM    788  CB  GLU A 132       7.878  23.056 -52.233  1.00  0.84
ATOM    789  CG  GLU A 132       7.433  21.586 -52.045  1.00  0.84
ATOM    790  CD  GLU A 132       6.048  21.496 -51.405  1.00  0.84
ATOM    791  OE1 GLU A 132       5.839  22.108 -50.326  1.00  0.84
ATOM    792  OE2 GLU A 132       5.169  20.836 -52.017  1.00  0.84
ATOM    793  N   MET A 133      10.002  25.190 -54.469  1.00  0.84
ATOM    794  CA  MET A 133      10.170  26.545 -54.923  1.00  0.84
ATOM    795  C   MET A 133       9.467  26.712 -56.250  1.00  0.84
ATOM    796  O   MET A 133       9.954  26.357 -57.322  1.00  0.84
ATOM    797  CB  MET A 133      11.661  26.927 -55.026  1.00  0.84
ATOM    798  CG  MET A 133      12.334  27.108 -53.652  1.00  0.84
ATOM    799  SD  MET A 133      11.865  28.619 -52.776  1.00  0.84
ATOM    800  CE  MET A 133      12.723  29.759 -53.907  1.00  0.84
ATOM    801  N   THR A 134       8.244  27.255 -56.176  1.00  0.79
ATOM    802  CA  THR A 134       7.429  27.612 -57.326  1.00  0.79
ATOM    803  C   THR A 134       7.976  28.845 -58.015  1.00  0.79
ATOM    804  O   THR A 134       8.669  29.642 -57.387  1.00  0.79
ATOM    805  CB  THR A 134       5.964  27.764 -56.949  1.00  0.79
ATOM    806  OG1 THR A 134       5.121  27.826 -58.082  1.00  0.79
ATOM    807  CG2 THR A 134       5.697  29.010 -56.095  1.00  0.79
ATOM    808  N   SER A 135       7.749  28.997 -59.334  1.00  0.79
ATOM    809  CA  SER A 135       8.293  30.082 -60.160  1.00  0.79
ATOM    810  C   SER A 135       9.816  30.079 -60.359  1.00  0.79
ATOM    811  O   SER A 135      10.333  30.753 -61.241  1.00  0.79
ATOM    812  CB  SER A 135       7.934  31.531 -59.685  1.00  0.79
ATOM    813  OG  SER A 135       6.569  31.707 -59.296  1.00  0.79
ATOM    814  N   LEU A 136      10.600  29.348 -59.537  1.00  0.81
ATOM    815  CA  LEU A 136      12.053  29.326 -59.584  1.00  0.81
ATOM    816  C   LEU A 136      12.629  28.584 -60.790  1.00  0.81
ATOM    817  O   LEU A 136      12.423  27.386 -60.972  1.00  0.81
ATOM    818  CB  LEU A 136      12.613  28.733 -58.261  1.00  0.81
ATOM    819  CG  LEU A 136      14.113  28.994 -57.983  1.00  0.81
ATOM    820  CD1 LEU A 136      14.366  30.454 -57.591  1.00  0.81
ATOM    821  CD2 LEU A 136      14.649  28.082 -56.869  1.00  0.81
ATOM    822  N   LYS A 137      13.390  29.295 -61.643  1.00  0.80
ATOM    823  CA  LYS A 137      13.860  28.828 -62.928  1.00  0.80
ATOM    824  C   LYS A 137      15.319  28.429 -62.929  1.00  0.80
ATOM    825  O   LYS A 137      15.716  27.559 -63.698  1.00  0.80
ATOM    826  CB  LYS A 137      13.718  29.967 -63.960  1.00  0.80
ATOM    827  CG  LYS A 137      12.275  30.463 -64.056  1.00  0.80
ATOM    828  CD  LYS A 137      12.097  31.575 -65.090  1.00  0.80
ATOM    829  CE  LYS A 137      10.656  32.076 -65.087  1.00  0.80
ATOM    830  NZ  LYS A 137      10.530  33.263 -65.950  1.00  0.80
ATOM    831  N   ASP A 138      16.149  29.003 -62.045  1.00  0.83
ATOM    832  CA  ASP A 138      17.547  28.650 -61.983  1.00  0.83
ATOM    833  C   ASP A 138      18.150  28.887 -60.606  1.00  0.83
ATOM    834  O   ASP A 138      17.677  29.681 -59.786  1.00  0.83
ATOM    835  CB  ASP A 138      18.380  29.331 -63.093  1.00  0.83
ATOM    836  CG  ASP A 138      18.289  30.825 -63.117  1.00  0.83
ATOM    837  OD1 ASP A 138      17.356  31.458 -63.668  1.00  0.83
ATOM    838  OD2 ASP A 138      19.311  31.375 -62.630  1.00  0.83
ATOM    839  N   ILE A 139      19.258  28.177 -60.314  1.00  0.82
ATOM    840  CA  ILE A 139      20.086  28.462 -59.159  1.00  0.82
ATOM    841  C   ILE A 139      21.087  29.518 -59.587  1.00  0.82
ATOM    842  O   ILE A 139      22.191  29.233 -60.036  1.00  0.82
ATOM    843  CB  ILE A 139      20.819  27.243 -58.588  1.00  0.82
ATOM    844  CG1 ILE A 139      19.844  26.122 -58.156  1.00  0.82
ATOM    845  CG2 ILE A 139      21.704  27.654 -57.385  1.00  0.82
ATOM    846  CD1 ILE A 139      19.659  25.040 -59.228  1.00  0.82
ATOM    847  N   GLY A 140      20.736  30.807 -59.439  1.00  0.85
ATOM    848  CA  GLY A 140      21.538  31.897 -59.981  1.00  0.85
ATOM    849  C   GLY A 140      22.747  32.288 -59.174  1.00  0.85
ATOM    850  O   GLY A 140      23.295  33.371 -59.344  1.00  0.85
ATOM    851  N   LEU A 141      23.209  31.427 -58.256  1.00  0.81
ATOM    852  CA  LEU A 141      24.360  31.668 -57.405  1.00  0.81
ATOM    853  C   LEU A 141      25.676  31.533 -58.164  1.00  0.81
ATOM    854  O   LEU A 141      26.500  30.666 -57.894  1.00  0.81
ATOM    855  CB  LEU A 141      24.364  30.713 -56.180  1.00  0.81
ATOM    856  CG  LEU A 141      23.096  30.767 -55.300  1.00  0.81
ATOM    857  CD1 LEU A 141      23.182  29.736 -54.161  1.00  0.81
ATOM    858  CD2 LEU A 141      22.859  32.170 -54.720  1.00  0.81
ATOM    859  N   TYR A 142      25.914  32.427 -59.142  1.00  0.78
ATOM    860  CA  TYR A 142      26.997  32.323 -60.100  1.00  0.78
ATOM    861  C   TYR A 142      28.382  32.590 -59.549  1.00  0.78
ATOM    862  O   TYR A 142      29.392  32.205 -60.141  1.00  0.78
ATOM    863  CB  TYR A 142      26.717  33.147 -61.390  1.00  0.78
ATOM    864  CG  TYR A 142      26.235  34.559 -61.149  1.00  0.78
ATOM    865  CD1 TYR A 142      27.081  35.546 -60.615  1.00  0.78
ATOM    866  CD2 TYR A 142      24.933  34.928 -61.530  1.00  0.78
ATOM    867  CE1 TYR A 142      26.630  36.865 -60.454  1.00  0.78
ATOM    868  CE2 TYR A 142      24.478  36.242 -61.359  1.00  0.78
ATOM    869  CZ  TYR A 142      25.325  37.209 -60.814  1.00  0.78
ATOM    870  OH  TYR A 142      24.872  38.532 -60.636  1.00  0.78
ATOM    871  N   ASN A 143      28.445  33.204 -58.362  1.00  0.82
ATOM    872  CA  ASN A 143      29.670  33.385 -57.626  1.00  0.82
ATOM    873  C   ASN A 143      29.904  32.287 -56.594  1.00  0.82
ATOM    874  O   ASN A 143      30.926  32.308 -55.915  1.00  0.82
ATOM    875  CB  ASN A 143      29.635  34.759 -56.916  1.00  0.82
ATOM    876  CG  ASN A 143      29.927  35.858 -57.930  1.00  0.82
ATOM    877  OD1 ASN A 143      30.846  35.744 -58.745  1.00  0.82
ATOM    878  ND2 ASN A 143      29.164  36.968 -57.885  1.00  0.82
ATOM    879  N   LEU A 144      29.023  31.266 -56.466  1.00  0.84
ATOM    880  CA  LEU A 144      29.215  30.169 -55.528  1.00  0.84
ATOM    881  C   LEU A 144      30.411  29.295 -55.888  1.00  0.84
ATOM    882  O   LEU A 144      30.527  28.778 -56.998  1.00  0.84
ATOM    883  CB  LEU A 144      27.929  29.317 -55.405  1.00  0.84
ATOM    884  CG  LEU A 144      27.928  28.201 -54.337  1.00  0.84
ATOM    885  CD1 LEU A 144      27.996  28.757 -52.905  1.00  0.84
ATOM    886  CD2 LEU A 144      26.676  27.326 -54.500  1.00  0.84
ATOM    887  N   ARG A 145      31.360  29.127 -54.944  1.00  0.80
ATOM    888  CA  ARG A 145      32.636  28.511 -55.245  1.00  0.80
ATOM    889  C   ARG A 145      33.013  27.397 -54.303  1.00  0.80
ATOM    890  O   ARG A 145      33.761  26.506 -54.694  1.00  0.80
ATOM    891  CB  ARG A 145      33.782  29.547 -55.114  1.00  0.80
ATOM    892  CG  ARG A 145      33.874  30.604 -56.229  1.00  0.80
ATOM    893  CD  ARG A 145      33.836  30.035 -57.651  1.00  0.80
ATOM    894  NE  ARG A 145      34.552  31.022 -58.525  1.00  0.80
ATOM    895  CZ  ARG A 145      35.871  30.968 -58.771  1.00  0.80
ATOM    896  NH1 ARG A 145      36.637  30.035 -58.212  1.00  0.80
ATOM    897  NH2 ARG A 145      36.428  31.866 -59.581  1.00  0.80
ATOM    898  N   ASN A 146      32.544  27.401 -53.046  1.00  0.83
ATOM    899  CA  ASN A 146      32.880  26.326 -52.144  1.00  0.83
ATOM    900  C   ASN A 146      31.724  26.116 -51.184  1.00  0.83
ATOM    901  O   ASN A 146      31.188  27.053 -50.591  1.00  0.83
ATOM    902  CB  ASN A 146      34.241  26.612 -51.442  1.00  0.83
ATOM    903  CG  ASN A 146      34.717  25.479 -50.534  1.00  0.83
ATOM    904  OD1 ASN A 146      34.161  25.236 -49.468  1.00  0.83
ATOM    905  ND2 ASN A 146      35.808  24.783 -50.924  1.00  0.83
ATOM    906  N   ILE A 147      31.313  24.851 -51.027  1.00  0.81
ATOM    907  CA  ILE A 147      30.442  24.404 -49.968  1.00  0.81
ATOM    908  C   ILE A 147      31.253  23.411 -49.159  1.00  0.81
ATOM    909  O   ILE A 147      31.544  22.301 -49.603  1.00  0.81
ATOM    910  CB  ILE A 147      29.131  23.805 -50.482  1.00  0.81
ATOM    911  CG1 ILE A 147      28.313  24.889 -51.237  1.00  0.81
ATOM    912  CG2 ILE A 147      28.336  23.221 -49.291  1.00  0.81
ATOM    913  CD1 ILE A 147      26.934  24.438 -51.745  1.00  0.81
ATOM    914  N   THR A 148      31.677  23.822 -47.946  1.00  0.78
ATOM    915  CA  THR A 148      32.715  23.149 -47.170  1.00  0.78
ATOM    916  C   THR A 148      32.361  21.748 -46.703  1.00  0.78
ATOM    917  O   THR A 148      33.187  20.837 -46.746  1.00  0.78
ATOM    918  CB  THR A 148      33.152  23.967 -45.951  1.00  0.78
ATOM    919  OG1 THR A 148      33.350  25.330 -46.294  1.00  0.78
ATOM    920  CG2 THR A 148      34.487  23.465 -45.383  1.00  0.78
ATOM    921  N   ARG A 149      31.118  21.540 -46.216  1.00  0.73
ATOM    922  CA  ARG A 149      30.769  20.348 -45.454  1.00  0.73
ATOM    923  C   ARG A 149      29.644  19.506 -46.037  1.00  0.73
ATOM    924  O   ARG A 149      29.874  18.418 -46.561  1.00  0.73
ATOM    925  CB  ARG A 149      30.445  20.738 -43.984  1.00  0.73
ATOM    926  CG  ARG A 149      30.270  19.541 -43.018  1.00  0.73
ATOM    927  CD  ARG A 149      30.038  19.981 -41.565  1.00  0.73
ATOM    928  NE  ARG A 149      29.804  18.758 -40.733  1.00  0.73
ATOM    929  CZ  ARG A 149      29.765  18.785 -39.394  1.00  0.73
ATOM    930  NH1 ARG A 149      29.920  19.910 -38.706  1.00  0.73
ATOM    931  NH2 ARG A 149      29.555  17.656 -38.719  1.00  0.73
ATOM    932  N   GLY A 150      28.375  19.933 -45.869  1.00  0.81
ATOM    933  CA  GLY A 150      27.230  19.091 -46.196  1.00  0.81
ATOM    934  C   GLY A 150      26.888  18.981 -47.649  1.00  0.81
ATOM    935  O   GLY A 150      27.403  19.692 -48.505  1.00  0.81
ATOM    936  N   ALA A 151      25.920  18.094 -47.927  1.00  0.82
ATOM    937  CA  ALA A 151      25.411  17.826 -49.251  1.00  0.82
ATOM    938  C   ALA A 151      24.272  18.766 -49.619  1.00  0.82
ATOM    939  O   ALA A 151      23.880  19.657 -48.866  1.00  0.82
ATOM    940  CB  ALA A 151      24.945  16.361 -49.361  1.00  0.82
ATOM    941  N   MET A 152      23.716  18.605 -50.823  1.00  0.85
ATOM    942  CA  MET A 152      22.670  19.458 -51.338  1.00  0.85
ATOM    943  C   MET A 152      21.399  18.689 -51.642  1.00  0.85
ATOM    944  O   MET A 152      21.418  17.602 -52.223  1.00  0.85
ATOM    945  CB  MET A 152      23.192  20.152 -52.605  1.00  0.85
ATOM    946  CG  MET A 152      22.219  21.136 -53.268  1.00  0.85
ATOM    947  SD  MET A 152      22.924  21.938 -54.727  1.00  0.85
ATOM    948  CE  MET A 152      22.804  20.451 -55.760  1.00  0.85
ATOM    949  N   ARG A 153      20.243  19.265 -51.245  1.00  0.86
ATOM    950  CA  ARG A 153      18.940  18.740 -51.587  1.00  0.86
ATOM    951  C   ARG A 153      18.143  19.747 -52.409  1.00  0.86
ATOM    952  O   ARG A 153      17.767  20.814 -51.931  1.00  0.86
ATOM    953  CB  ARG A 153      18.162  18.302 -50.326  1.00  0.86
ATOM    954  CG  ARG A 153      17.007  17.327 -50.635  1.00  0.86
ATOM    955  CD  ARG A 153      16.391  16.693 -49.379  1.00  0.86
ATOM    956  NE  ARG A 153      16.478  15.198 -49.445  1.00  0.86
ATOM    957  CZ  ARG A 153      15.433  14.373 -49.579  1.00  0.86
ATOM    958  NH1 ARG A 153      14.197  14.778 -49.814  1.00  0.86
ATOM    959  NH2 ARG A 153      15.633  13.067 -49.427  1.00  0.86
ATOM    960  N   ILE A 154      17.865  19.440 -53.691  1.00  0.86
ATOM    961  CA  ILE A 154      17.071  20.297 -54.569  1.00  0.86
ATOM    962  C   ILE A 154      15.888  19.488 -55.068  1.00  0.86
ATOM    963  O   ILE A 154      16.052  18.525 -55.816  1.00  0.86
ATOM    964  CB  ILE A 154      17.858  20.853 -55.760  1.00  0.86
ATOM    965  CG1 ILE A 154      19.028  21.750 -55.295  1.00  0.86
ATOM    966  CG2 ILE A 154      16.913  21.650 -56.682  1.00  0.86
ATOM    967  CD1 ILE A 154      19.842  22.354 -56.450  1.00  0.86
ATOM    968  N   GLU A 155      14.652  19.846 -54.674  1.00  0.85
ATOM    969  CA  GLU A 155      13.533  18.944 -54.861  1.00  0.85
ATOM    970  C   GLU A 155      12.213  19.659 -55.092  1.00  0.85
ATOM    971  O   GLU A 155      11.967  20.759 -54.605  1.00  0.85
ATOM    972  CB  GLU A 155      13.472  18.005 -53.634  1.00  0.85
ATOM    973  CG  GLU A 155      12.510  16.799 -53.688  1.00  0.85
ATOM    974  CD  GLU A 155      12.424  16.137 -52.323  1.00  0.85
ATOM    975  OE1 GLU A 155      13.202  16.528 -51.410  1.00  0.85
ATOM    976  OE2 GLU A 155      11.604  15.201 -52.175  1.00  0.85
ATOM    977  N   LYS A 156      11.325  19.043 -55.896  1.00  0.85
ATOM    978  CA  LYS A 156       9.985  19.526 -56.206  1.00  0.85
ATOM    979  C   LYS A 156       9.912  20.940 -56.767  1.00  0.85
ATOM    980  O   LYS A 156       9.046  21.736 -56.413  1.00  0.85
ATOM    981  CB  LYS A 156       9.002  19.330 -55.027  1.00  0.85
ATOM    982  CG  LYS A 156       8.663  17.861 -54.750  1.00  0.85
ATOM    983  CD  LYS A 156       7.677  17.748 -53.577  1.00  0.85
ATOM    984  CE  LYS A 156       7.623  16.338 -52.983  1.00  0.85
ATOM    985  NZ  LYS A 156       6.669  16.271 -51.864  1.00  0.85
ATOM    986  N   ASN A 157      10.809  21.279 -57.707  1.00  0.85
ATOM    987  CA  ASN A 157      10.810  22.594 -58.316  1.00  0.85
ATOM    988  C   ASN A 157      10.467  22.466 -59.798  1.00  0.85
ATOM    989  O   ASN A 157      11.364  22.225 -60.612  1.00  0.85
ATOM    990  CB  ASN A 157      12.179  23.281 -58.136  1.00  0.85
ATOM    991  CG  ASN A 157      12.592  23.230 -56.671  1.00  0.85
ATOM    992  OD1 ASN A 157      11.937  23.758 -55.779  1.00  0.85
ATOM    993  ND2 ASN A 157      13.721  22.550 -56.396  1.00  0.85
ATOM    994  N   PRO A 158       9.211  22.621 -60.229  1.00  0.83
ATOM    995  CA  PRO A 158       8.776  22.105 -61.527  1.00  0.83
ATOM    996  C   PRO A 158       9.211  22.984 -62.675  1.00  0.83
ATOM    997  O   PRO A 158       9.062  22.580 -63.826  1.00  0.83
ATOM    998  CB  PRO A 158       7.240  22.058 -61.415  1.00  0.83
ATOM    999  CG  PRO A 158       6.896  23.068 -60.318  1.00  0.83
ATOM   1000  CD  PRO A 158       8.066  22.903 -59.356  1.00  0.83
ATOM   1001  N   GLU A 159       9.734  24.187 -62.394  1.00  0.78
ATOM   1002  CA  GLU A 159      10.201  25.107 -63.403  1.00  0.78
ATOM   1003  C   GLU A 159      11.714  25.239 -63.424  1.00  0.78
ATOM   1004  O   GLU A 159      12.272  25.861 -64.328  1.00  0.78
ATOM   1005  CB  GLU A 159       9.533  26.475 -63.168  1.00  0.78
ATOM   1006  CG  GLU A 159       8.004  26.371 -63.395  1.00  0.78
ATOM   1007  CD  GLU A 159       7.260  27.700 -63.468  1.00  0.78
ATOM   1008  OE1 GLU A 159       7.902  28.778 -63.429  1.00  0.78
ATOM   1009  OE2 GLU A 159       6.013  27.617 -63.599  1.00  0.78
ATOM   1010  N   LEU A 160      12.413  24.595 -62.466  1.00  0.82
ATOM   1011  CA  LEU A 160      13.842  24.738 -62.267  1.00  0.82
ATOM   1012  C   LEU A 160      14.690  24.085 -63.340  1.00  0.82
ATOM   1013  O   LEU A 160      14.598  22.891 -63.598  1.00  0.82
ATOM   1014  CB  LEU A 160      14.244  24.204 -60.873  1.00  0.82
ATOM   1015  CG  LEU A 160      15.575  24.734 -60.301  1.00  0.82
ATOM   1016  CD1 LEU A 160      15.469  26.216 -59.933  1.00  0.82
ATOM   1017  CD2 LEU A 160      15.964  23.956 -59.039  1.00  0.82
ATOM   1018  N   CYS A 161      15.556  24.871 -63.982  1.00  0.82
ATOM   1019  CA  CYS A 161      16.447  24.477 -65.043  1.00  0.82
ATOM   1020  C   CYS A 161      17.869  24.665 -64.548  1.00  0.82
ATOM   1021  O   CYS A 161      18.094  25.053 -63.403  1.00  0.82
ATOM   1022  CB  CYS A 161      16.187  25.337 -66.312  1.00  0.82
ATOM   1023  SG  CYS A 161      14.928  24.622 -67.413  1.00  0.82
ATOM   1024  N   TYR A 162      18.870  24.332 -65.396  1.00  0.78
ATOM   1025  CA  TYR A 162      20.285  24.502 -65.088  1.00  0.78
ATOM   1026  C   TYR A 162      20.763  23.655 -63.905  1.00  0.78
ATOM   1027  O   TYR A 162      21.468  24.118 -63.011  1.00  0.78
ATOM   1028  CB  TYR A 162      20.692  25.998 -64.905  1.00  0.78
ATOM   1029  CG  TYR A 162      20.477  26.806 -66.162  1.00  0.78
ATOM   1030  CD1 TYR A 162      21.496  26.931 -67.121  1.00  0.78
ATOM   1031  CD2 TYR A 162      19.257  27.462 -66.393  1.00  0.78
ATOM   1032  CE1 TYR A 162      21.298  27.681 -68.288  1.00  0.78
ATOM   1033  CE2 TYR A 162      19.037  28.176 -67.579  1.00  0.78
ATOM   1034  CZ  TYR A 162      20.056  28.275 -68.527  1.00  0.78
ATOM   1035  OH  TYR A 162      19.820  28.955 -69.732  1.00  0.78
ATOM   1036  N   LEU A 163      20.376  22.361 -63.872  1.00  0.80
ATOM   1037  CA  LEU A 163      20.773  21.447 -62.811  1.00  0.80
ATOM   1038  C   LEU A 163      21.992  20.620 -63.192  1.00  0.80
ATOM   1039  O   LEU A 163      22.869  20.362 -62.370  1.00  0.80
ATOM   1040  CB  LEU A 163      19.630  20.469 -62.428  1.00  0.80
ATOM   1041  CG  LEU A 163      18.268  21.147 -62.174  1.00  0.80
ATOM   1042  CD1 LEU A 163      17.333  20.966 -63.379  1.00  0.80
ATOM   1043  CD2 LEU A 163      17.582  20.603 -60.913  1.00  0.80
ATOM   1044  N   ASP A 164      22.085  20.209 -64.469  1.00  0.78
ATOM   1045  CA  ASP A 164      23.097  19.349 -65.034  1.00  0.78
ATOM   1046  C   ASP A 164      24.214  20.166 -65.679  1.00  0.78
ATOM   1047  O   ASP A 164      25.285  19.660 -66.004  1.00  0.78
ATOM   1048  CB  ASP A 164      22.426  18.448 -66.120  1.00  0.78
ATOM   1049  CG  ASP A 164      21.572  19.191 -67.159  1.00  0.78
ATOM   1050  OD1 ASP A 164      21.062  20.313 -66.888  1.00  0.78
ATOM   1051  OD2 ASP A 164      21.399  18.624 -68.264  1.00  0.78
ATOM   1052  N   SER A 165      23.997  21.488 -65.800  1.00  0.82
ATOM   1053  CA  SER A 165      24.975  22.470 -66.246  1.00  0.82
ATOM   1054  C   SER A 165      25.863  22.947 -65.126  1.00  0.82
ATOM   1055  O   SER A 165      26.834  23.667 -65.352  1.00  0.82
ATOM   1056  CB  SER A 165      24.305  23.762 -66.778  1.00  0.82
ATOM   1057  OG  SER A 165      23.386  24.303 -65.830  1.00  0.82
ATOM   1058  N   VAL A 166      25.548  22.587 -63.876  1.00  0.85
ATOM   1059  CA  VAL A 166      26.346  22.989 -62.747  1.00  0.85
ATOM   1060  C   VAL A 166      27.162  21.802 -62.336  1.00  0.85
ATOM   1061  O   VAL A 166      26.664  20.755 -61.927  1.00  0.85
ATOM   1062  CB  VAL A 166      25.536  23.494 -61.571  1.00  0.85
ATOM   1063  CG1 VAL A 166      26.481  23.921 -60.426  1.00  0.85
ATOM   1064  CG2 VAL A 166      24.677  24.682 -62.040  1.00  0.85
ATOM   1065  N   ASP A 167      28.485  21.946 -62.439  1.00  0.82
ATOM   1066  CA  ASP A 167      29.396  20.952 -61.962  1.00  0.82
ATOM   1067  C   ASP A 167      29.587  21.160 -60.477  1.00  0.82
ATOM   1068  O   ASP A 167      30.220  22.108 -60.016  1.00  0.82
ATOM   1069  CB  ASP A 167      30.682  21.083 -62.784  1.00  0.82
ATOM   1070  CG  ASP A 167      31.753  20.093 -62.393  1.00  0.82
ATOM   1071  OD1 ASP A 167      32.160  20.115 -61.206  1.00  0.82
ATOM   1072  OD2 ASP A 167      32.189  19.337 -63.292  1.00  0.82
ATOM   1073  N   TRP A 168      28.981  20.259 -59.692  1.00  0.76
ATOM   1074  CA  TRP A 168      28.984  20.362 -58.260  1.00  0.76
ATOM   1075  C   TRP A 168      30.215  19.706 -57.649  1.00  0.76
ATOM   1076  O   TRP A 168      30.509  19.944 -56.482  1.00  0.76
ATOM   1077  CB  TRP A 168      27.677  19.745 -57.685  1.00  0.76
ATOM   1078  CG  TRP A 168      26.377  20.351 -58.230  1.00  0.76
ATOM   1079  CD1 TRP A 168      25.572  19.871 -59.229  1.00  0.76
ATOM   1080  CD2 TRP A 168      25.767  21.570 -57.769  1.00  0.76
ATOM   1081  NE1 TRP A 168      24.508  20.718 -59.434  1.00  0.76
ATOM   1082  CE2 TRP A 168      24.597  21.765 -58.554  1.00  0.76
ATOM   1083  CE3 TRP A 168      26.120  22.486 -56.783  1.00  0.76
ATOM   1084  CZ2 TRP A 168      23.784  22.868 -58.351  1.00  0.76
ATOM   1085  CZ3 TRP A 168      25.302  23.609 -56.594  1.00  0.76
ATOM   1086  CH2 TRP A 168      24.144  23.796 -57.365  1.00  0.76
ATOM   1087  N   SER A 169      31.004  18.924 -58.421  1.00  0.75
ATOM   1088  CA  SER A 169      32.194  18.229 -57.933  1.00  0.75
ATOM   1089  C   SER A 169      33.339  19.172 -57.600  1.00  0.75
ATOM   1090  O   SER A 169      34.145  18.924 -56.706  1.00  0.75
ATOM   1091  CB  SER A 169      32.675  17.112 -58.905  1.00  0.75
ATOM   1092  OG  SER A 169      33.342  17.609 -60.069  1.00  0.75
ATOM   1093  N   PHE A 170      33.396  20.334 -58.281  1.00  0.72
ATOM   1094  CA  PHE A 170      34.322  21.398 -57.943  1.00  0.72
ATOM   1095  C   PHE A 170      33.729  22.463 -57.032  1.00  0.72
ATOM   1096  O   PHE A 170      34.396  23.448 -56.725  1.00  0.72
ATOM   1097  CB  PHE A 170      34.807  22.107 -59.232  1.00  0.72
ATOM   1098  CG  PHE A 170      35.597  21.170 -60.103  1.00  0.72
ATOM   1099  CD1 PHE A 170      35.310  21.097 -61.474  1.00  0.72
ATOM   1100  CD2 PHE A 170      36.603  20.337 -59.577  1.00  0.72
ATOM   1101  CE1 PHE A 170      35.973  20.177 -62.293  1.00  0.72
ATOM   1102  CE2 PHE A 170      37.256  19.405 -60.392  1.00  0.72
ATOM   1103  CZ  PHE A 170      36.937  19.322 -61.751  1.00  0.72
ATOM   1104  N   ILE A 171      32.478  22.306 -56.553  1.00  0.79
ATOM   1105  CA  ILE A 171      31.886  23.264 -55.620  1.00  0.79
ATOM   1106  C   ILE A 171      31.748  22.627 -54.245  1.00  0.79
ATOM   1107  O   ILE A 171      31.848  23.299 -53.222  1.00  0.79
ATOM   1108  CB  ILE A 171      30.517  23.772 -56.086  1.00  0.79
ATOM   1109  CG1 ILE A 171      30.575  24.296 -57.540  1.00  0.79
ATOM   1110  CG2 ILE A 171      30.023  24.910 -55.156  1.00  0.79
ATOM   1111  CD1 ILE A 171      29.183  24.555 -58.128  1.00  0.79
ATOM   1112  N   MET A 172      31.565  21.298 -54.163  1.00  0.78
ATOM   1113  CA  MET A 172      31.465  20.597 -52.898  1.00  0.78
ATOM   1114  C   MET A 172      32.099  19.232 -52.980  1.00  0.78
ATOM   1115  O   MET A 172      32.260  18.661 -54.054  1.00  0.78
ATOM   1116  CB  MET A 172      30.001  20.393 -52.456  1.00  0.78
ATOM   1117  CG  MET A 172      29.169  19.459 -53.356  1.00  0.78
ATOM   1118  SD  MET A 172      27.461  19.294 -52.778  1.00  0.78
ATOM   1119  CE  MET A 172      26.924  20.903 -53.406  1.00  0.78
ATOM   1120  N   ASN A 173      32.464  18.649 -51.826  1.00  0.73
ATOM   1121  CA  ASN A 173      33.181  17.391 -51.800  1.00  0.73
ATOM   1122  C   ASN A 173      32.284  16.157 -51.866  1.00  0.73
ATOM   1123  O   ASN A 173      32.533  15.210 -52.604  1.00  0.73
ATOM   1124  CB  ASN A 173      34.053  17.314 -50.523  1.00  0.73
ATOM   1125  CG  ASN A 173      35.126  18.396 -50.567  1.00  0.73
ATOM   1126  OD1 ASN A 173      35.682  18.731 -51.611  1.00  0.73
ATOM   1127  ND2 ASN A 173      35.468  18.962 -49.388  1.00  0.73
ATOM   1128  N   THR A 174      31.191  16.110 -51.084  1.00  0.72
ATOM   1129  CA  THR A 174      30.373  14.913 -50.901  1.00  0.72
ATOM   1130  C   THR A 174      29.286  14.770 -51.937  1.00  0.72
ATOM   1131  O   THR A 174      28.126  14.506 -51.625  1.00  0.72
ATOM   1132  CB  THR A 174      29.740  14.837 -49.518  1.00  0.72
ATOM   1133  OG1 THR A 174      29.257  16.121 -49.147  1.00  0.72
ATOM   1134  CG2 THR A 174      30.810  14.403 -48.507  1.00  0.72
ATOM   1135  N   GLU A 175      29.657  14.848 -53.228  1.00  0.71
ATOM   1136  CA  GLU A 175      28.754  14.739 -54.360  1.00  0.71
ATOM   1137  C   GLU A 175      27.915  13.473 -54.346  1.00  0.71
ATOM   1138  O   GLU A 175      26.719  13.497 -54.627  1.00  0.71
ATOM   1139  CB  GLU A 175      29.493  14.929 -55.708  1.00  0.71
ATOM   1140  CG  GLU A 175      30.408  13.772 -56.189  1.00  0.71
ATOM   1141  CD  GLU A 175      31.028  14.091 -57.551  1.00  0.71
ATOM   1142  OE1 GLU A 175      30.286  14.591 -58.437  1.00  0.71
ATOM   1143  OE2 GLU A 175      32.246  13.829 -57.710  1.00  0.71
SPDBVT        1.0000000000         0.0000000000         0.0000000000 
SPDBVT        0.0000000000         1.0000000000         0.0000000000 
SPDBVT        0.0000000000         0.0000000000         1.0000000000 
SPDBVT        0.0000000000         0.0000000000         0.0000000000 
SPDBVT        0.0000000000         0.0000000000         0.0000000000 
SPDBVV default;
SPDBVV      2.884198722130    1134.256363923542      20.000000000000
SPDBVV        0.8633539277        -0.4937879037         0.1038917782 
SPDBVV        0.2777525752         0.6369368281         0.7191418386 
SPDBVV       -0.4212760406        -0.5920177220         0.6870527741 
SPDBVV       17.2490000000       -24.7960000000       -65.3230000000 
SPDBVV        0.0000000000         0.0000000000         0.0000000000 
SPDBVf 19 19 19 19 19 19 19 19 19 19 19 19 19 19 19 19 19 19 19 19
SPDBVf 19 19 19 19 19 19 19 19 19 19 19 19 19 19 19 19 19 19 19 19
SPDBVf 19 19 19 19 19 19 19 19 19 19 19 19 19 19 19 19 19 19 19 19
SPDBVf 19 19 19 19 19 19 19 19 19 19 19 19 19 19 19 19 19 19 19 19
SPDBVf 19 19 19 19 19 19 19 19 19 19 19 19 19 19 19 19 19 19 19 19
SPDBVf 19 19 19 19 19 19 19 19 19 19 19 19 19 19 19 19 19 19 19 19
SPDBVf 19 19 19 19 19 19 19 19 19 19 19 19 19 19 19 19 19 19 19 19
SPDBVf 19
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 
SPDBVb 0.00 0.00 0.20
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64
SPDBVi        1 1 1 0 1 0 1 1 0 1 0 1 1 0  0
SPDBVp        0
END



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elNémo is maintained by Yves-Henri Sanejouand.
It was developed by Karsten Suhre.
Between 2003 and 2014, it was hosted by IGS (Marseille).
Last modification: October 18th, 2018.